Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T47101 Target Info
Target Name Fibroblast growth factor receptor 1 (FGFR1)
Synonyms c-fgr; bFGF-R-1; bFGF-R; N-sam; HBGFR; Fms-like tyrosine kinase 2; FLT2; FLT-2; FLG; FGFR-1; FGFBR; CEK; CD331 antigen; CD331; Basic fibroblast growth factor receptor 1; BFGFR
Target Type Successful Target
Gene Name FGFR1
Biochemical Class Kinase
UniProt ID
FGFR1_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: Pemigatinib Ligand Info
Structure Description Crystal structure of FGFR1 kinase domain with Pemigatinib PDB:7WCL
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [1]
PDB Sequence
GVSEYELPED
468
PRWELPRDRL
478
VLGKPLGEGC
488
FGQVVLAEAI
498
GLDKDKPNRV
508

TKVAVKMLKS
518
DATEKDLSDL
528
ISEMEMMKMI
538
GKHKNIINLL
548
GACTQDGPLY
558

VIVEYASKGN
568
LREYLQARRP
578
PGLEYSYNPS
588
HNPEEQLSSK
598
DLVSCAYQVA
608

RGMEYLASKK
618
CIHRDLAARN
628
VLVTEDNVMK
638
IADFGLARDI
648
HHIDYYKKTT
658

NGRLPVKWMA
668
PEALFDRIYT
678
HQSDVWSFGV
688
LLWEIFTLGG
698
SPYPGVPVEE
708

LFKLLKEGHR
718
MDKPSNCTNE
728
LYMMMRDCWH
738
AVPSQRPTFK
748
QLVEDLDRIV
758

ALTSNQ
Residue
Distance (Å)
LYS482
3.457
PRO483
4.496
LEU484
3.530
GLY485
4.894
VAL492
3.525
ALA512
3.569
VAL513
4.537
LYS514
3.143
LEU528
4.864
GLU531
3.405
MET535
3.862
ILE545
3.786
VAL559
3.703
Residue
Distance (Å)
VAL561
3.439
GLU562
3.292
TYR563
3.634
ALA564
2.844
SER565
3.668
LYS566
4.841
GLY567
3.883
LEU630
3.489
ILE639
4.602
ALA640
3.184
ASP641
2.899
PHE642
3.829
Ligand Name: Erdafitinib Ligand Info
Structure Description FIBROBLAST GROWTH FACTOR RECEPTOR 1 IN COMPLEX WITH JNJ-4275693 PDB:5EW8
Method X-ray diffraction Resolution 1.63 Å Mutation No [2]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKD
503
KPNRVTKVAV
513

KMLKSDATEK
523
DLSDLISEME
533
MMKMIGKHKN
543
IINLLGACTQ
553
DGPLYVIVEY
563

ASKGNLREYL
573
QARRPPGEEQ
594
LSSKDLVSCA
604
YQVARGMEYL
614
ASKKCIHRDL
624

AARNVLVTED
634
NVMKIADFGL
644
ARDIHHIDYY
654
KKTTNGRLPV
664
KWMAPEALFD
674

RIYTHQSDVW
684
SFGVLLWEIF
694
TLGGSPYPGV
704
PVEELFKLLK
714
EGHRMDKPSN
724

CTNELYMMMR
734
DCWHAVPSQR
744
PTFKQLVEDL
754
DRIVALTSNQ
764
E
Residue
Distance (Å)
LEU484
2.711
GLY485
4.374
VAL492
3.100
ALA512
3.278
LYS514
3.348
LEU528
4.048
GLU531
2.611
MET535
2.920
ILE545
2.719
ASN546
4.597
LEU547
4.972
VAL559
3.038
VAL561
2.893
GLU562
2.282
TYR563
3.047
Residue
Distance (Å)
ALA564
2.288
SER565
3.184
LYS566
4.034
GLY567
3.296
GLU571
3.871
ARG627
2.608
ASN628
2.877
VAL629
4.687
LEU630
3.357
ILE639
3.470
ALA640
3.131
ASP641
2.661
PHE642
2.810
GLY643
4.790
Ligand Name: Lenvatinib Ligand Info
Structure Description FGFR-1 in complex with ligand lenvatinib PDB:5ZV2
Method X-ray diffraction Resolution 2.86 Å Mutation Yes [3]
PDB Sequence
YELPEDPRWE
472
LPRDRLVLGK
482
PLGEGAFGQV
492
VLAEAIGLDK
502
DKPNRVTKVA
512

VKMLKSDATE
522
KDLSDLISEM
532
EMMKMIGKHK
542
NIINLLGACT
552
QDGPLYVIVE
562

YASKGNLREY
572
LQARRPEQLS
596
SKDLVSCAYQ
606
VARGMEYLAS
616
KKCIHRDLAA
626

RNVLVTEDNV
636
MKIADFGLAR
646
DHIDYYKKTT
658
NGRLPVKWMA
668
PEALFDRIYT
678

HQSDVWSFGV
688
LLWEIFTLGG
698
SPYPGVPVEE
708
LFKLLKEGHR
718
MDKPSNCTNE
728

LYMMMRDCWH
738
AVPSQRPTFK
748
QLVEDLDRIV
758
ALTS
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .LEV or .LEV2 or .LEV3 or :3LEV;style chemicals stick;color identity;select .A:484 or .A:485 or .A:489 or .A:492 or .A:512 or .A:514 or .A:531 or .A:534 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:567 or .A:568 or .A:571 or .A:630 or .A:640 or .A:641 or .A:642 or .A:644; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.957
GLY485
2.980
PHE489
3.429
VAL492
3.912
ALA512
3.311
LYS514
3.586
GLU531
3.167
MET534
4.612
MET535
3.468
ILE545
4.100
VAL559
4.814
VAL561
3.928
Residue
Distance (Å)
GLU562
3.194
TYR563
3.735
ALA564
3.040
SER565
3.852
GLY567
3.309
ASN568
4.757
GLU571
4.366
LEU630
3.494
ALA640
3.750
ASP641
3.203
PHE642
3.304
LEU644
4.447
Ligand Name: BGJ398 Ligand Info
Structure Description Co-structure of Fibroblast Growth Factor Receptor 1 kinase domain with 3-(2,6-dichloro-3,5-dimethoxy-phenyl)-1-{6-[4-(4-ethyl-piperazin-1-yl)-phenylamino]-pyrimidin-4-yl}-1-methyl-urea (BGJ398) PDB:3TT0
Method X-ray diffraction Resolution 2.80 Å Mutation Yes [4]
PDB Sequence
SEYELPEDPR
470
WELPRDRLVL
480
GKPLGEGAFG
490
QVVLAEAIGL
500
DKDKPNRVTK
510

VAVKMLKSDA
520
TEKDLSDLIS
530
EMEMMKMIGK
540
HKNIINLLGA
550
CTQDGPLYVI
560

VEYASKGNLR
570
EYLQARRPPG
580
LEYSYNPSHN
590
PEEQLSSKDL
600
VSCAYQVARG
610

MEYLASKKCI
620
HRDLAARNVL
630
VTEDNVMKIA
640
DFGLARDIHH
650
IDYYKKTTNG
660

RLPVKWMAPE
670
ALFDRIYTHQ
680
SDVWSFGVLL
690
WEIFTLGGSP
700
YPGVPVEELF
710

KLLKEGHRMD
720
KPSNCTNELY
730
MMMRDCWHAV
740
PSQRPTFKQL
750
VEDLDRIVAL
760

TSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .07J or .07J2 or .07J3 or :307J;style chemicals stick;color identity;select .A:484 or .A:485 or .A:492 or .A:512 or .A:513 or .A:514 or .A:528 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:567 or .A:568 or .A:571 or .A:630 or .A:640 or .A:641 or .A:642 or .A:643; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.743
GLY485
4.780
VAL492
3.220
ALA512
3.525
VAL513
4.301
LYS514
3.363
LEU528
4.962
GLU531
3.679
MET535
3.475
ILE545
3.621
VAL559
3.651
VAL561
3.359
Residue
Distance (Å)
GLU562
3.479
TYR563
3.685
ALA564
2.718
SER565
4.326
GLY567
3.699
ASN568
4.336
GLU571
3.551
LEU630
3.730
ALA640
3.236
ASP641
3.213
PHE642
4.257
GLY643
4.590
Ligand Name: AZD4547 Ligand Info
Structure Description Structure of FGFR1 in complex with AZD4547 (N-{3-[2-(3,5-DIMETHOXYPHENYL)ETHYL]-1H-PYRAZOL-5-YL}-4-[(3R,5S)-3,5-DIMETHYLPIPERAZIN-1-YL]BENZAMIDE) at 1.65 angstrom PDB:4WUN
Method X-ray diffraction Resolution 1.65 Å Mutation No [5]
PDB Sequence
LPEDPRWELP
474
RDRLVLGKPL
484
GEGAFGQVVL
494
AEAIGLDKDK
504
PNRVTKVAVK
514

MLKSDATEKD
524
LSDLISEMEM
534
MKMIGKHKNI
544
INLLGACTQD
554
GPLYVIVEYA
564

SKGNLREYLQ
574
ARRPPLEYSY
585
NPSHNPEEQL
595
SSKDLVSCAY
605
QVARGMEYLA
615

SKKCIHRDLA
625
ARNVLVTEDN
635
VMKIADFGLP
663
VKWMAPEALF
673
DRIYTHQSDV
683

WSFGVLLWEI
693
FTLGGSPYPG
703
VPVEELFKLL
713
KEGHRMDKPS
723
NCTNELYMMM
733

RDCWHAVPSQ
743
RPTFKQLVED
753
LDRIVALTSN
763
QE
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .66T or .66T2 or .66T3 or :366T;style chemicals stick;color identity;select .A:484 or .A:485 or .A:489 or .A:492 or .A:512 or .A:514 or .A:528 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:568 or .A:571 or .A:630 or .A:639 or .A:640 or .A:641 or .A:642 or .A:643; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.655
GLY485
3.646
PHE489
3.809
VAL492
4.174
ALA512
3.456
LYS514
3.389
LEU528
4.698
GLU531
3.453
MET535
3.239
ILE545
3.799
VAL559
3.698
VAL561
3.565
GLU562
2.799
Residue
Distance (Å)
TYR563
3.675
ALA564
2.987
SER565
3.487
LYS566
3.846
GLY567
3.411
ASN568
4.588
GLU571
3.302
LEU630
3.662
ILE639
4.914
ALA640
3.606
ASP641
2.887
PHE642
3.748
GLY643
4.584
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Ligand Name: TAS-120 Ligand Info
Structure Description TAS-120 in reversible binding mode with FGFR1 PDB:6MZQ
Method X-ray diffraction Resolution 2.00 Å Mutation No [6]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGQVVLAE
496
AIGLDKDKPN
506
RVTKVAVKML
516

KSDATEKDLS
526
DLISEMEMMK
536
MIGKHKNIIN
546
LLGACTQDGP
556
LYVIVEYASK
566

GNLREYLQAR
576
RPPGLEYSYN
586
PSEEQLSSKD
599
LVSCAYQVAR
609
GMEYLASKKC
619

IHRDLAARNV
629
LVTEDNVMKI
639
ADFGLPVKWM
667
APEALFDRIY
677
THQSDVWSFG
687

VLLWEIFTLG
697
GSPYPGVPVE
707
ELFKLLKEGH
717
RMDKPSNCTN
727
ELYMMMRDCW
737

HAVPSQRPTF
747
KQLVEDLDRI
757
VALTSQE
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .TZ0 or .TZ02 or .TZ03 or :3TZ0;style chemicals stick;color identity;select .A:484 or .A:485 or .A:492 or .A:512 or .A:514 or .A:528 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:567 or .A:568 or .A:571 or .A:627 or .A:630 or .A:639 or .A:640 or .A:641 or .A:642; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.324
GLY485
4.140
VAL492
3.773
ALA512
3.458
LYS514
2.957
LEU528
4.836
GLU531
3.476
MET535
3.628
ILE545
3.561
VAL559
3.841
VAL561
3.760
GLU562
2.742
Residue
Distance (Å)
TYR563
3.461
ALA564
2.783
SER565
4.675
GLY567
4.215
ASN568
2.927
GLU571
4.122
ARG627
3.266
LEU630
3.469
ILE639
4.639
ALA640
3.502
ASP641
2.909
PHE642
3.569
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Ligand Name: TKI258 Ligand Info
Structure Description Native FGFR1 with an inhibitor PDB:5AM6
Method X-ray diffraction Resolution 1.96 Å Mutation No [7]
PDB Sequence
VAGVSEYELP
466
EDPRWELPRD
476
RLVLGKPLGE
486
GQVVLAEAIG
499
LDKDKPNRVT
509

KVAVKMLKSD
519
ATEKDLSDLI
529
SEMEMMKMIG
539
KHKNIINLLG
549
ACTQDGPLYV
559

IVEYASKGNL
569
REYLQARRPP
579
GEEQLSSKDL
600
VSCAYQVARG
610
MEYLASKKCI
620

HRDLAARNVL
630
VTEDNVMKIA
640
DFGLARDIHH
650
IDYYKKTTNG
660
RLPVKWMAPE
670

ALFDRIYTHQ
680
SDVWSFGVLL
690
WEIFTLGGSP
700
YPGVPVEELF
710
KLLKEGHRMD
720

KPSNCTNELY
730
MMMRDCWHAV
740
PSQRPTFKQL
750
VEDLDRIVAL
760
TSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .38O or .38O2 or .38O3 or :338O;style chemicals stick;color identity;select .A:482 or .A:484 or .A:492 or .A:512 or .A:514 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:630 or .A:640 or .A:641; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS482
4.212
LEU484
3.724
VAL492
3.899
ALA512
3.689
LYS514
3.893
ILE545
3.804
VAL561
3.501
GLU562
3.047
Residue
Distance (Å)
TYR563
3.315
ALA564
2.543
SER565
3.459
LYS566
3.696
GLY567
3.468
LEU630
3.456
ALA640
4.636
ASP641
3.854
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Ligand Name: Debio 1347 Ligand Info
Structure Description Human FGFR1 kinase in complex with CH5183284 PDB:5B7V
Method X-ray diffraction Resolution 2.15 Å Mutation Yes [8]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEQVVLAEA
497
IGLDKDKPNR
507
VTKVAVKMLK
517

SDATEKDLSD
527
LISEMEMMKM
537
IGKHKNIINL
547
LGACTQDGPL
557
YVIVEYASKG
567

NLREYLQARR
577
PPPEEQLSSK
598
DLVSCAYQVA
608
RGMEYLASKK
618
CIHRDLAARN
628

VLVTEDNVMK
638
IADFGLARHI
651
DYYKKTTNGR
661
LPVKWMAPEA
671
LFDRIYTHQS
681

DVWSFGVLLW
691
EIFTLGGSPY
701
PGVPVEELFK
711
LLKEGHRMDK
721
PSNCTNELYM
731

MMRDCWHAVP
741
SQRPTFKQLV
751
EDLDRIVALT
761
SN
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .LWJ or .LWJ2 or .LWJ3 or :3LWJ;style chemicals stick;color identity;select .A:484 or .A:485 or .A:492 or .A:512 or .A:514 or .A:531 or .A:535 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:630 or .A:640 or .A:641 or .A:642 or .A:643; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.710
GLY485
4.891
VAL492
3.794
ALA512
3.596
LYS514
3.950
GLU531
2.872
MET535
3.741
ILE545
3.778
VAL561
3.604
GLU562
2.863
Residue
Distance (Å)
TYR563
3.545
ALA564
2.659
SER565
3.370
LYS566
4.545
GLY567
3.608
LEU630
3.552
ALA640
3.821
ASP641
2.981
PHE642
3.617
GLY643
3.735
Ligand Name: Decavanadate Ligand Info
Structure Description Crystal Structure of activated receptor tyrosine kinase in complex with substrates PDB:3GQI
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [9]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKD
503
KPNRVTKVAV
513

KMLKSDATEK
523
DLSDLISEME
533
MMKMIGKHKN
543
IINLLGACTQ
553
DGPLYVIVEY
563

ASKGNLREYL
573
QARRPPGLEF
583
SFNPSHNPEE
593
QLSSKDLVSC
603
AYQVARGMEY
613

LASKKCIHRD
623
LAARNVLVTE
633
DNVMKIADFG
643
LARDIHHIDK
655
KTTNGRLPVK
665

WMAPEALFDR
675
IYTHQSDVWS
685
FGVLLWEIFT
695
LGGSPYPGVP
705
VEELFKLLKE
715

GHRMDKPSNC
725
TNELYMMMRD
735
CWHAVPSQRP
745
TFKQLVEDLD
755
RIVALTSNQE
765

LDLS
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .DVT or .DVT2 or .DVT3 or :3DVT;style chemicals stick;color identity;select .A:503 or .A:504 or .A:505 or .A:506 or .A:507; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP503
3.081
LYS504
3.058
PRO505
3.390
Residue
Distance (Å)
ASN506
2.625
ARG507
3.004
Ligand Name: L-betagamma-meATP Ligand Info
Structure Description Crystal Structure of activated receptor tyrosine kinase in complex with substrates PDB:3GQI
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [9]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKD
503
KPNRVTKVAV
513

KMLKSDATEK
523
DLSDLISEME
533
MMKMIGKHKN
543
IINLLGACTQ
553
DGPLYVIVEY
563

ASKGNLREYL
573
QARRPPGLEF
583
SFNPSHNPEE
593
QLSSKDLVSC
603
AYQVARGMEY
613

LASKKCIHRD
623
LAARNVLVTE
633
DNVMKIADFG
643
LARDIHHIDK
655
KTTNGRLPVK
665

WMAPEALFDR
675
IYTHQSDVWS
685
FGVLLWEIFT
695
LGGSPYPGVP
705
VEELFKLLKE
715

GHRMDKPSNC
725
TNELYMMMRD
735
CWHAVPSQRP
745
TFKQLVEDLD
755
RIVALTSNQE
765

LDLS
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ACP or .ACP2 or .ACP3 or :3ACP;style chemicals stick;color identity;select .A:484 or .A:485 or .A:486 or .A:487 or .A:488 or .A:489 or .A:490 or .A:492 or .A:512 or .A:514 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:567 or .A:568 or .A:571 or .A:627 or .A:628 or .A:630 or .A:641; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.405
GLY485
3.173
GLU486
4.214
GLY487
3.272
ALA488
3.107
PHE489
3.137
GLY490
3.460
VAL492
3.561
ALA512
3.349
LYS514
3.442
ILE545
4.702
Residue
Distance (Å)
VAL561
4.102
GLU562
3.048
TYR563
3.814
ALA564
3.193
GLY567
4.551
ASN568
3.153
GLU571
4.045
ARG627
2.898
ASN628
3.138
LEU630
3.524
ASP641
2.539
Ligand Name: Phosphonotyrosine Ligand Info
Structure Description Crystal Structure of activated receptor tyrosine kinase in complex with substrates PDB:3GQI
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [9]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKD
503
KPNRVTKVAV
513

KMLKSDATEK
523
DLSDLISEME
533
MMKMIGKHKN
543
IINLLGACTQ
553
DGPLYVIVEY
563

ASKGNLREYL
573
QARRPPGLEF
583
SFNPSHNPEE
593
QLSSKDLVSC
603
AYQVARGMEY
613

LASKKCIHRD
623
LAARNVLVTE
633
DNVMKIADFG
643
LARDIHHIDK
655
KTTNGRLPVK
665

WMAPEALFDR
675
IYTHQSDVWS
685
FGVLLWEIFT
695
LGGSPYPGVP
705
VEELFKLLKE
715

GHRMDKPSNC
725
TNELYMMMRD
735
CWHAVPSQRP
745
TFKQLVEDLD
755
RIVALTSNQE
765

LDLS
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .PTR or .PTR2 or .PTR3 or :3PTR;style chemicals stick;color identity;select .A:620 or .A:622 or .A:646 or .A:648 or .A:651 or .A:652 or .A:655 or .A:656 or .A:657 or .A:658 or .A:675 or .A:676 or .A:677 or .A:678 or .A:764 or .A:765 or .A:767 or .A:768; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE620
3.761
ARG622
3.516
ARG646
2.964
ILE648
3.608
ILE651
3.039
ASP652
1.335
LYS655
1.336
LYS656
2.753
THR657
3.228
Residue
Distance (Å)
THR658
3.743
ARG675
3.662
ILE676
3.804
TYR677
2.821
THR678
3.848
GLN764
3.321
GLU765
1.324
LEU767
1.329
ASP768
3.385
Ligand Name: PD173074 Ligand Info
Structure Description CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF FGF RECEPTOR 1 IN COMPLEX WITH INHIBITOR PD173074 PDB:2FGI
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [10]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGQVVLAEAI
498
GLPNRVTKVA
512
VKMLKSDATE
522

KDLSDLISEM
532
EMMKMIGKHK
542
NIINLLGACT
552
QDGPLYVIVE
562
YASKGNLREY
572

LQARRPPQLS
596
SKDLVSCAYQ
606
VARGMEYLAS
616
KKCIHRDLAA
626
RNVLVTEDNV
636

MKIADFGLAD
647
IHHIDYYKKT
657
NGRLPVKWMA
668
PEALFDRIYT
678
HQSDVWSFGV
688

LLWEIFTLGG
698
SPYPGVPVEE
708
LFKLLKEGHR
718
MDKPSNCTNE
728
LYMMMRDCWH
738

AVPSQRPTFK
748
QLVEDLDRIV
758
ALTS
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .PD1 or .PD12 or .PD13 or :3PD1;style chemicals stick;color identity;select .A:482 or .A:484 or .A:485 or .A:492 or .A:512 or .A:514 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:630 or .A:639 or .A:640 or .A:641 or .A:642; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS482
3.929
LEU484
3.496
GLY485
3.212
VAL492
3.569
ALA512
3.756
LYS514
2.779
GLU531
3.878
MET535
3.238
ILE545
3.693
VAL559
3.596
VAL561
3.517
Residue
Distance (Å)
GLU562
3.359
TYR563
3.405
ALA564
2.543
SER565
3.263
LYS566
4.540
GLY567
3.495
LEU630
3.426
ILE639
4.757
ALA640
3.611
ASP641
2.993
PHE642
3.617
Ligand Name: SU5402 Ligand Info
Structure Description CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF FIBROBLAST GROWTH FACTOR RECEPTOR 1 IN COMPLEX WITH SU5402 INHIBITOR PDB:1FGI
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [11]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLPNR
507
VTKVAVKMLK
517

SDATEKDLSD
527
LISEMEMMKM
537
IGKHKNIINL
547
LGACTQDGPL
557
YVIVEYASKG
567

NLREYLQARR
577
PPEEQLSSKD
599
LVSCAYQVAR
609
GMEYLASKKC
619
IHRDLAARNV
629

LVTEDNVMKI
639
ADFGLARDIH
649
HIDYYKKTTN
659
GRLPVKWMAP
669
EALFDRIYTH
679

QSDVWSFGVL
689
LWEIFTLGGS
699
PYPGVPVEEL
709
FKLLKEGHRM
719
DKPSNCTNEL
729

YMMMRDCWHA
739
VPSQRPTFKQ
749
LVEDLDRIVA
759
LTS
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SU1 or .SU12 or .SU13 or :3SU1;style chemicals stick;color identity;select .A:484 or .A:485 or .A:486 or .A:488 or .A:489 or .A:492 or .A:512 or .A:514 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:568 or .A:571 or .A:627 or .A:630 or .A:640; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.771
GLY485
3.498
GLU486
4.335
ALA488
4.404
PHE489
3.682
VAL492
4.007
ALA512
3.275
LYS514
4.197
ILE545
3.655
VAL561
3.463
GLU562
2.869
Residue
Distance (Å)
TYR563
3.180
ALA564
2.758
SER565
3.731
LYS566
4.663
GLY567
3.406
ASN568
2.783
GLU571
4.639
ARG627
4.709
LEU630
3.417
ALA640
4.861
Ligand Name: Propanoic acid Ligand Info
Structure Description Fibroblast growth factor receptor 1 kinase in complex with JK-P3 PDB:4UWC
Method X-ray diffraction Resolution 1.96 Å Mutation Yes [12]
PDB Sequence
LPEDPRWELP
474
RDRLVLGKPL
484
GEGAFGQVVL
494
AEAIGLDKDK
504
PNRVTKVAVK
514

MLKSDATEKD
524
LSDLISEMEM
534
MKMIGKHKNI
544
INLLGACTQD
554
GPLYVIVEYA
564

SKGNLREYLQ
574
ARRPPGLEYS
584
YNPSHNPEEQ
594
LSSKDLVSCA
604
YQVARGMEYL
614

ASKKCIHRDL
624
AARNVLVTED
634
NVMKIADFGL
644
ARDIHHIDYY
654
KKTTNGRLPV
664

KWMAPEALFD
674
RIYTHQSDVW
684
SFGVLLWEIF
694
TLGGSPYPGV
704
PVEELFKLLK
714

EGHRMDKPSN
724
CTNELYMMMR
734
DCWHAVPSQR
744
PTFKQLVEDL
754
DRIVALTSNQ
764

E
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .PPI or .PPI2 or .PPI3 or :3PPI;style chemicals stick;color identity;select .A:565 or .A:566 or .A:567 or .A:571 or .A:572 or .A:574 or .A:575 or .A:576 or .A:577 or .A:593 or .A:695 or .A:697 or .A:698 or .A:699 or .A:702; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER565
4.847
LYS566
3.002
GLY567
4.861
GLU571
4.700
TYR572
3.543
GLN574
4.122
ALA575
4.635
ARG576
2.820
Residue
Distance (Å)
ARG577
2.921
GLU593
4.687
THR695
4.988
GLY697
4.185
GLY698
3.623
SER699
3.238
PRO702
4.485
Ligand Name: 3-(3-methoxybenzyl)-1H-pyrrolo[2,3-b]pyridine Ligand Info
Structure Description FGFR TYROSINE KINASE DOMAIN IN COMPLEX WITH 3-(3-methoxybenzyl)-7-azaindole PDB:3C4F
Method X-ray diffraction Resolution 2.07 Å Mutation Yes [13]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKD
503
KPNRVTKVAV
513

KMLKSDATEK
523
DLSDLISEME
533
MMKMIGKHKN
543
IINLLGACTQ
553
DGPLYVIVEY
563

ASKGNLREYL
573
QARRPPEEQL
595
SSKDLVSCAY
605
QVARGMEYLA
615
SKKCIHRDLA
625

ARNVLVTEDN
635
VMKIADFGLA
645
RDIHHIDYYK
655
KTTNGRLPVK
665
WMAPEALFDR
675

IYTHQSDVWS
685
FGVLLWEIFT
695
LGGSPYPGVP
705
VEELFKLLKE
715
GHRMDKPSNC
725

TNELYMMMRD
735
CWHAVPSQRP
745
TFKQLVEDLD
755
RIVALTSNQE
765
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .C4F or .C4F2 or .C4F3 or :3C4F;style chemicals stick;color identity;select .A:484 or .A:485 or .A:489 or .A:492 or .A:512 or .A:514 or .A:531 or .A:535 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:630 or .A:639 or .A:640 or .A:641 or .A:642; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.999
GLY485
4.265
PHE489
3.418
VAL492
4.296
ALA512
3.338
LYS514
3.720
GLU531
4.182
MET535
3.763
ILE545
3.732
Residue
Distance (Å)
VAL561
3.576
GLU562
2.893
TYR563
3.803
ALA564
3.005
LEU630
3.544
ILE639
4.836
ALA640
3.471
ASP641
2.963
PHE642
3.849
Ligand Name: 8-Cyclohexyl-N-Methoxy-5-Oxo-2-{[4-(2-Pyrrolidin-1-Ylethyl)phenyl]amino}-5,8-Dihydropyrido[2,3-D]pyrimidine-6-Carboxamide Ligand Info
Structure Description cFMS tyrosine kinase in complex with a pyridopyrimidinone inhibitor PDB:3DPK
Method X-ray diffraction Resolution 1.95 Å Mutation No [14]
PDB Sequence
VRWKIIESSY
561
TFIDPYNEKW
575
EFPRNNLQFG
585
KTLGAGAFGK
595
VVEATAFGLG
605

AVLKVAVKML
618
KSTAHADEKE
628
ALMSELKIMS
638
HLGQHENIVN
648
LLGACTHGGP
658

VLVITEYCCY
668
GDLLNFLRRQ
696
LSSRDLLHFS
759
SQVAQGMAFL
769
ASKNCIHRDV
779

AARNVLLTNG
789
HVAKIGDFGL
799
ARDIMNDSNY
809
IVRLPVKWMA
823
PESIFDCVYT
833

VQSDVWSYGI
843
LLWEIFSLGL
853
NPYPGILVNS
863
KFYKLVKDGY
873
QMAQPAFAPK
883

NIYSIMQACW
893
ALEPTHRPTF
903
QQICSFLQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .8C5 or .8C52 or .8C53 or :38C5;style chemicals stick;color identity;select .A:586 or .A:587 or .A:588 or .A:589 or .A:590 or .A:596 or .A:614 or .A:616 or .A:633 or .A:637 or .A:647 or .A:661 or .A:663 or .A:664 or .A:665 or .A:666 or .A:667 or .A:668 or .A:669 or .A:670 or .A:673 or .A:782 or .A:783 or .A:785 or .A:786 or .A:795 or .A:796 or .A:797 or .A:800 or .A:801 or .A:802; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS586
3.055
THR587
3.026
LEU588
2.285
GLY589
2.199
ALA590
3.939
VAL596
2.605
ALA614
2.896
LYS616
1.937
GLU633
2.811
MET637
2.331
VAL647
2.453
VAL661
4.037
THR663
2.213
GLU664
2.138
TYR665
2.635
CYS666
2.036
Residue
Distance (Å)
CYS667
3.530
TYR668
4.816
GLY669
2.769
ASP670
3.792
ASN673
4.882
ARG782
3.565
ASN783
4.088
LEU785
2.250
LEU786
4.975
GLY795
4.159
ASP796
2.707
PHE797
2.421
ALA800
2.944
ARG801
2.743
ASP802
4.543
Ligand Name: 4-Cyano-N-(2-Cyclohex-1-En-1-Yl-4-Piperidin-4-Ylphenyl)-1h-Imidazole-2-Carboxamide Ligand Info
Structure Description cFMS tyrosine kinase in complex with 4-Cyano-1H-imidazole-2-carboxylic acid (2-cyclohex-1-enyl-4-piperidin-4-yl-phenyl)-amide PDB:3KRJ
Method X-ray diffraction Resolution 2.10 Å Mutation Yes [15]
PDB Sequence
PKYQVRWKII
553
ESYEGNSYTF
563
IDPTQLPYNE
573
KWEFPRNNLQ
583
FGKTLGAGAF
593

GKVVEATAFG
603
LGKEDAVLKV
613
AVKMLKSTAH
623
ADEKEALMSE
633
LKIMSHLGQH
643

ENIVNLLGAC
653
THGGPVLVIT
663
EYCCYGDLLN
673
FLRRKRPPGQ
696
LSSRDLLHFS
759

SQVAQGMAFL
769
ASKNCIHRDV
779
AARNVLLTNG
789
HVAKIGDFGL
799
ARDIMNDSNY
809

IVKGARLPVK
820
WMAPESIFDC
830
VYTVQSDVWS
840
YGILLWEIFS
850
LGLNPYPGIL
860

VNSKFYKLVK
870
DGYQMAQPAF
880
APKNIYSIMQ
890
ACWALEPTHR
900
PTFQQICSFL
910

QEQA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KRJ or .KRJ2 or .KRJ3 or :3KRJ;style chemicals stick;color identity;select .A:588 or .A:589 or .A:596 or .A:598 or .A:614 or .A:616 or .A:647 or .A:663 or .A:664 or .A:665 or .A:666 or .A:667 or .A:668 or .A:669 or .A:670 or .A:673 or .A:782 or .A:785 or .A:796 or .A:797 or .A:799 or .A:800 or .A:801; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU588
1.904
GLY589
3.583
VAL596
2.841
GLU598
4.697
ALA614
3.005
LYS616
3.064
VAL647
2.500
THR663
1.733
GLU664
2.046
TYR665
2.425
CYS666
2.132
CYS667
2.520
Residue
Distance (Å)
TYR668
3.035
GLY669
2.277
ASP670
1.914
ASN673
4.047
ARG782
4.227
LEU785
2.268
ASP796
4.246
PHE797
2.996
LEU799
4.518
ALA800
2.449
ARG801
2.456
Ligand Name: 5-Cyano-N-[4-(4-Methylpiperazin-1-Yl)-2-Piperidin-1-Ylphenyl]furan-2-Carboxamide Ligand Info
Structure Description cFMS Tyrosine kinase in complex with 5-Cyano-furan-2-carboxylic acid [4-(4-methyl-piperazin-1-yl)-2-piperidin-1-yl-phenyl]-amide PDB:3KRL
Method X-ray diffraction Resolution 2.40 Å Mutation Yes [15]
PDB Sequence
KYQVRWKIIP
570
YNEKWEFPRN
580
NLQFGKTLGA
590
GAFGKVVEAT
600
AFGLGKEDAV
610

LKVAVKMLKS
620
TAADEKEALM
631
SELKIMSHLG
641
QHENIVNLLG
651
ACTHGGPVLV
661

ITEYCCYGDL
671
LNFLRRKRQL
697
SSRDLLHFSS
760
QVAQGMAFLA
770
SKNCIHRDVA
780

ARNVLLTNGH
790
VAKIGDFGLA
800
RDIMNDSNYI
810
VKGARLPVKW
821
MAPESIFDCV
831

YTVQSDVWSY
841
GILLWEIFSL
851
GLNPYPGILV
861
NSKFYKLVKD
871
GYQMAQPAFA
881

PKNIYSIMQA
891
CWALEPTHRP
901
TFQQICSFLQ
911
E
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KRL or .KRL2 or .KRL3 or :3KRL;style chemicals stick;color identity;select .A:586 or .A:588 or .A:589 or .A:596 or .A:614 or .A:616 or .A:647 or .A:663 or .A:664 or .A:665 or .A:666 or .A:667 or .A:668 or .A:669 or .A:670 or .A:677 or .A:782 or .A:785 or .A:796 or .A:797 or .A:799 or .A:800 or .A:801; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS586
1.903
LEU588
2.174
GLY589
2.571
VAL596
2.993
ALA614
3.353
LYS616
2.335
VAL647
2.484
THR663
1.942
GLU664
2.242
TYR665
2.430
CYS666
2.194
CYS667
3.219
Residue
Distance (Å)
TYR668
3.490
GLY669
2.604
ASP670
2.710
ARG677
3.787
ARG782
4.693
LEU785
2.513
ASP796
4.263
PHE797
2.538
LEU799
4.383
ALA800
2.424
ARG801
2.557
Ligand Name: (E)-[4-(3,5-Difluorophenyl)-3h-Pyrrolo[2,3-B]pyridin-3-Ylidene](3-Methoxyphenyl)methanol Ligand Info
Structure Description Crystal Structure of activated receptor tyrosine kinase in complex with substrates PDB:3GQL
Method X-ray diffraction Resolution 2.80 Å Mutation Yes [9]
PDB Sequence
YELPEDPRWE
472
LPRDRLVLGK
482
PLGEGAFGQV
492
VLAEAIGLDK
502
DKPNRVTKVA
512

VKMLKSDATE
522
KDLSDLISEM
532
EMMKMIGKHK
542
NIINLLGACT
552
QDGPLYVIVE
562

YASKGNLREY
572
LQARRPPEQL
595
SSKDLVSCAY
605
QVARGMEYLA
615
SKKCIHRDLA
625

ARNVLVTEDN
635
VMKIADFGLA
645
RNGRLPVKWM
667
APEALFDRIY
677
THQSDVWSFG
687

VLLWEIFTLG
697
GSPYPGVPVE
707
ELFKLLKEGH
717
RMDKPSNCTN
727
ELYMMMRDCW
737

HAVPSQRPTF
747
KQLVEDLDRI
757
VALTSNQEYL
767
DLSMPLD
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GQL or .GQL2 or .GQL3 or :3GQL;style chemicals stick;color identity;select .A:484 or .A:485 or .A:486 or .A:487 or .A:491 or .A:492 or .A:512 or .A:514 or .A:531 or .A:535 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:630 or .A:639 or .A:640 or .A:641 or .A:642; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.546
GLY485
3.477
GLU486
3.314
GLY487
3.872
GLN491
4.950
VAL492
3.091
ALA512
3.299
LYS514
3.624
GLU531
3.540
MET535
4.250
Residue
Distance (Å)
ILE545
3.308
VAL561
3.802
GLU562
2.737
TYR563
3.348
ALA564
3.089
LEU630
3.435
ILE639
4.701
ALA640
4.091
ASP641
3.118
PHE642
3.947
Ligand Name: 5-(Thiophen-2-yl)nicotinic Acid Ligand Info
Structure Description Crystal structure of minimal kinase domain of fibroblast growth factor receptor 1 in complex with 5-(2-thienyl)nicotinic acid PDB:3JS2
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [16]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKD
503
KPNRVTKVAV
513

KMLKSDATEK
523
DLSDLISEME
533
MMKMIGKHKN
543
IINLLGACTQ
553
DGPLYVIVEY
563

ASKGNLREYL
573
QARRPPGLHN
590
PEEQLSSKDL
600
VSCAYQVARG
610
MEYLASKKCI
620

HRDLAARNVL
630
VTEDNVMKIA
640
DFGLARDIHH
650
IDYYKKTTNG
660
RLPVKWMAPE
670

ALFDRIYTHQ
680
SDVWSFGVLL
690
WEIFTLGGSP
700
YPGVPVEELF
710
KLLKEGHRMD
720

KPSNCTNELY
730
MMMRDCWHAV
740
PSQRPTFKQL
750
VEDLDRIVAL
760
TSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .VM1 or .VM12 or .VM13 or :3VM1;style chemicals stick;color identity;select .A:484 or .A:489 or .A:492 or .A:512 or .A:514 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:567 or .A:630 or .A:640 or .A:641; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.160
PHE489
3.860
VAL492
4.238
ALA512
3.741
LYS514
4.278
ILE545
3.655
VAL561
3.377
Residue
Distance (Å)
GLU562
3.204
TYR563
3.463
ALA564
2.682
GLY567
4.327
LEU630
3.383
ALA640
4.739
ASP641
4.591
Ligand Name: 3-(2,6-dichloro-3,5-dimethoxyphenyl)-1-{(3S)-1-[(2E)-4-(dimethylamino)but-2-enoyl]pyrrolidin-3-yl}-7-(phenylamino)-3,4-dihydropyrimido[4,5-d]pyrimidin-2(1H)-one Ligand Info
Structure Description FGFR1 kinase complex with inhibitor SN37118 PDB:6C1B
Method X-ray diffraction Resolution 2.00 Å Mutation Yes [17]
PDB Sequence
LPEDPRWELP
474
RDRLVLGKPL
484
GQVVLAEAIG
499
LDKDKPNRVT
509
KVAVKMLKSD
519

ATEKDLSDLI
529
SEMEMMKMIG
539
KHKNIINLLG
549
ACTQDGPLYV
559
IVEYASKGNL
569

REYLQARRPE
592
EQLSSKDLVS
602
CAYQVARGME
612
YLASKKCIHR
622
DLAARNVLVT
632

EDNVMKIADF
642
GLPVKWMAPE
670
ALFDRIYTHQ
680
SDVWSFGVLL
690
WEIFTLGGSP
700

YPGVPVEELF
710
KLLKEGHRMD
720
KPSNCTNELY
730
MMMRDCWHAV
740
PSQRPTFKQL
750

VEDLDRIVAL
760
TSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .YY4 or .YY42 or .YY43 or :3YY4;style chemicals stick;color identity;select .A:484 or .A:485 or .A:492 or .A:512 or .A:513 or .A:514 or .A:528 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:568 or .A:571 or .A:627 or .A:630 or .A:640 or .A:641 or .A:642 or .A:643; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.300
GLY485
4.181
VAL492
3.436
ALA512
3.806
VAL513
4.404
LYS514
3.510
LEU528
4.994
GLU531
3.562
MET535
3.148
ILE545
3.804
VAL559
3.571
VAL561
3.584
GLU562
3.404
Residue
Distance (Å)
TYR563
3.887
ALA564
2.683
SER565
3.964
LYS566
4.691
GLY567
3.603
ASN568
3.082
GLU571
2.892
ARG627
4.603
LEU630
3.429
ALA640
3.208
ASP641
3.062
PHE642
3.926
GLY643
4.729
Ligand Name: 3-(2,6-dichloro-3,5-dimethoxyphenyl)-1-[(3S)-1-[(E)-4-(dimethylamino)but-2-enoyl]pyrrolidin-3-yl]-7-(methylamino)-4H-pyrimido[4,5-d]pyrimidin-2-one Ligand Info
Structure Description FGFR1 kinase complex with inhibitor SN36985 PDB:6C19
Method X-ray diffraction Resolution 2.12 Å Mutation No [18]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEQVVLAEA
497
IGLDKDKPNR
507
VTKVAVKMLK
517

SDATEKDLSD
527
LISEMEMMKM
537
IGKHKNIINL
547
LGACTQDGPL
557
YVIVEYASKG
567

NLREYLQARR
577
PPEYSYNPSE
592
EQLSSKDLVS
602
CAYQVARGME
612
YLASKKCIHR
622

DLAARNVLVT
632
EDNVMKIADF
642
GLLPVKWMAP
669
EALFDRIYTH
679
QSDVWSFGVL
689

LWEIFTLGGS
699
PYPGVPVEEL
709
FKLLKEGHRM
719
DKPSNCTNEL
729
YMMMRDCWHA
739

VPSQRPTFKQ
749
LVEDLDRIVA
759
LTSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .YY7 or .YY72 or .YY73 or :3YY7;style chemicals stick;color identity;select .A:484 or .A:485 or .A:492 or .A:512 or .A:513 or .A:514 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:567 or .A:568 or .A:571 or .A:627 or .A:630 or .A:640 or .A:641 or .A:642 or .A:643; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.305
GLY485
3.837
VAL492
3.582
ALA512
3.631
VAL513
4.465
LYS514
3.363
GLU531
3.388
MET535
3.377
ILE545
3.846
VAL559
3.618
VAL561
3.533
GLU562
3.303
Residue
Distance (Å)
TYR563
3.800
ALA564
2.906
GLY567
4.019
ASN568
3.003
GLU571
2.908
ARG627
4.790
LEU630
3.569
ALA640
3.202
ASP641
3.001
PHE642
3.837
GLY643
4.513
Ligand Name: 7-(cyclohexylamino)-3-(2,6-dichloro-3,5-dimethoxyphenyl)-1-[(3S)-1-[(E)-4-(dimethylamino)but-2-enoyl]pyrrolidin-3-yl]-4H-pyrimido[4,5-d]pyrimidin-2-one Ligand Info
Structure Description FGFR1 kinase complex with inhibitor SN37116 PDB:6C1C
Method X-ray diffraction Resolution 2.15 Å Mutation Yes [19]
PDB Sequence
LPEDPRWELP
474
RDRLVLGKPL
484
GEGQVVLAEA
497
IGLDKDKPNR
507
VTKVAVKMLK
517

SDATEKDLSD
527
LISEMEMMKM
537
IGKHKNIINL
547
LGACTQDGPL
557
YVIVEYASKG
567

NLREYLQARR
577
PPSYNPSHNP
591
EEQLSSKDLV
601
SCAYQVARGM
611
EYLASKKCIH
621

RDLAARNVLV
631
TEDNVMKIAD
641
FGLPVKWMAP
669
EALFDRIYTH
679
QSDVWSFGVL
689

LWEIFTLGGS
699
PYPGVPVEEL
709
FKLLKEGHRM
719
DKPSNCTNEL
729
YMMMRDCWHA
739

VPSQRPTFKQ
749
LVEDLDRIVA
759
LTSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .YY6 or .YY62 or .YY63 or :3YY6;style chemicals stick;color identity;select .A:484 or .A:485 or .A:492 or .A:512 or .A:513 or .A:514 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:567 or .A:568 or .A:571 or .A:627 or .A:630 or .A:640 or .A:641 or .A:642; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.610
GLY485
4.218
VAL492
3.588
ALA512
3.676
VAL513
4.432
LYS514
3.582
GLU531
3.588
MET535
3.829
ILE545
3.861
VAL559
3.495
VAL561
3.409
GLU562
3.387
Residue
Distance (Å)
TYR563
3.803
ALA564
2.632
SER565
4.653
GLY567
3.614
ASN568
3.236
GLU571
2.430
ARG627
4.459
LEU630
3.739
ALA640
3.297
ASP641
2.996
PHE642
3.620
Ligand Name: 7-anilino-3-(2,6-dichloro-3,5-dimethoxyphenyl)-1-[1-[(E)-4-(dimethylamino)but-2-enoyl]piperidin-4-yl]-4H-pyrimido[4,5-d]pyrimidin-2-one Ligand Info
Structure Description FGFR1 kinase domain complex with SN37333 in reversible binding mode PDB:5UR1
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [20]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGFGQVVL
494
AEAIGLDKDK
504
PNRVTKVAVK
514

MLKSDATEKD
524
LSDLISEMEM
534
MKMIGKHKNI
544
INLLGACTQD
554
GPLYVIVEYA
564

SKGNLREYLQ
574
ARRPPYNPSH
589
NPEEQLSSKD
599
LVSCAYQVAR
609
GMEYLASKKC
619

IHRDLAARNV
629
LVTEDNVMKI
639
ADFGLPVKWM
667
APEALFDRIY
677
THQSDVWSFG
687

VLLWEIFTLG
697
GSPYPGVPVE
707
ELFKLLKEGH
717
RMDKPSNCTN
727
ELYMMMRDCW
737

HAVPSQRPTF
747
KQLVEDLDRI
757
VALTSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .YY9 or .YY92 or .YY93 or :3YY9;style chemicals stick;color identity;select .A:484 or .A:485 or .A:486 or .A:487 or .A:492 or .A:512 or .A:513 or .A:514 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:568 or .A:630 or .A:640 or .A:641 or .A:642 or .A:643; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.375
GLY485
4.195
GLU486
3.498
GLY487
3.880
VAL492
3.364
ALA512
3.973
VAL513
4.473
LYS514
3.518
GLU531
3.461
MET535
3.850
ILE545
3.792
VAL559
3.558
VAL561
3.557
Residue
Distance (Å)
GLU562
3.509
TYR563
3.943
ALA564
2.673
SER565
4.422
LYS566
4.886
GLY567
3.675
ASN568
3.994
LEU630
3.759
ALA640
3.246
ASP641
3.005
PHE642
3.897
GLY643
4.762
Ligand Name: CID 53348188 Ligand Info
Structure Description FGFR1 kinase domain complexed with FIIN-1 PDB:6C1O
Method X-ray diffraction Resolution 2.29 Å Mutation Yes [21]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKD
503
KPNRVTKVAV
513

KMLKSDATEK
523
DLSDLISEME
533
MMKMIGKHKN
543
IINLLGACTQ
553
DGPLYVIVEY
563

ASKGNLREYL
573
QARRPPYNPS
588
HNPEEQLSSK
598
DLVSCAYQVA
608
RGMEYLASKK
618

CIHRDLAARN
628
VLVTEDNVMK
638
IADFGLLPVK
665
WMAPEALFDR
675
IYTHQSDVWS
685

FGVLLWEIFT
695
LGGSPYPGVP
705
VEELFKLLKE
715
GHRMDKPSNC
725
TNELYMMMRD
735

CWHAVPSQRP
745
TFKQLVEDLD
755
RIVALTSNQE
765
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MK9 or .MK92 or .MK93 or :3MK9;style chemicals stick;color identity;select .A:482 or .A:484 or .A:485 or .A:492 or .A:512 or .A:513 or .A:514 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:568 or .A:571 or .A:627 or .A:630 or .A:640 or .A:641 or .A:642; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS482
4.795
LEU484
3.526
GLY485
4.616
VAL492
3.378
ALA512
3.634
VAL513
4.427
LYS514
3.196
GLU531
3.247
MET535
3.393
ILE545
3.775
VAL559
3.553
VAL561
3.538
GLU562
3.397
Residue
Distance (Å)
TYR563
3.684
ALA564
2.757
SER565
3.815
LYS566
4.100
GLY567
3.337
ASN568
2.740
GLU571
4.200
ARG627
4.731
LEU630
3.620
ALA640
3.148
ASP641
3.005
PHE642
3.528
Ligand Name: 2,2-Dimethyl-2,3-Dihydro-1-Benzofuran-7-Carboxamide Ligand Info
Structure Description FGFR1 kinase domain complex with fragment 2,2-dimethyl-2,3-dihydrobenzofuran-7-carboxamide PDB:5UQ0
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [22]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEFGQVVLA
495
EAIGLDKPNR
507
VTKVAVKMLK
517

SDATEKDLSD
527
LISEMEMMKM
537
IGKHKNIINL
547
LGACTQDGPL
557
YVIVEYASKG
567

NLREYLQARR
577
PEQLSSKDLV
601
SCAYQVARGM
611
EYLASKKCIH
621
RDLAARNVLV
631

TEDNVMKIAD
641
FGLLPVKWMA
668
PEALFDRIYT
678
HQSDVWSFGV
688
LLWEIFTLGG
698

SPYPGVPVEL
709
FKLLKEGHRM
719
DKPSNCTNEL
729
YMMMRDCWHA
739
VPSQRPTFKQ
749

LVEDLDRIVA
759
LTSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .WP1 or .WP12 or .WP13 or :3WP1;style chemicals stick;color identity;select .A:484 or .A:485 or .A:492 or .A:512 or .A:514 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:630 or .A:640 or .A:641; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.662
GLY485
4.744
VAL492
3.950
ALA512
3.382
LYS514
4.907
ILE545
4.333
VAL561
4.084
Residue
Distance (Å)
GLU562
2.982
TYR563
3.547
ALA564
2.624
SER565
4.953
LEU630
3.632
ALA640
3.752
ASP641
3.553
Ligand Name: 3-(2,6-dichloro-3,5-dimethoxyphenyl)-1-{(3S)-1-[(2E)-4-(dimethylamino)but-2-enoyl]pyrrolidin-3-yl}-7-[(propan-2-yl)amino]-3,4-dihydropyrimido[4,5-d]pyrimidin-2(1H)-one Ligand Info
Structure Description FGFR1 kinase complex with inhibitor SN37115 PDB:6C18
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [23]
PDB Sequence
LPEDPRWELP
474
RDRLVLGKPL
484
GGQVVLAEAI
498
GLDKDKPNRV
508
TKVAVKMLKS
518

DATEKDLSDL
528
ISEMEMMKMI
538
GKHKNIINLL
548
GACTQDGPLY
558
VIVEYASKGN
568

LREYLQARRP
578
PGSYNPSHNP
591
EEQLSSKDLV
601
SCAYQVARGM
611
EYLASKKCIH
621

RDLAARNVLV
631
TEDNVMKIAD
641
FGLPVKWMAP
669
EALFDRIYTH
679
QSDVWSFGVL
689

LWEIFTLGGS
699
PYPGVPVEEL
709
FKLLKEGHRM
719
DKPSNCTNEL
729
YMMMRDCWHA
739

VPSQRPTFKQ
749
LVEDLDRIVA
759
LTSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .YY5 or .YY52 or .YY53 or :3YY5;style chemicals stick;color identity;select .A:484 or .A:485 or .A:492 or .A:512 or .A:513 or .A:514 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:567 or .A:568 or .A:571 or .A:627 or .A:630 or .A:639 or .A:640 or .A:641 or .A:642; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.398
GLY485
4.205
VAL492
3.635
ALA512
3.645
VAL513
4.553
LYS514
3.389
GLU531
3.426
MET535
3.119
ILE545
3.534
VAL559
3.623
VAL561
3.484
GLU562
3.242
Residue
Distance (Å)
TYR563
3.703
ALA564
2.712
SER565
4.793
GLY567
3.904
ASN568
2.983
GLU571
2.701
ARG627
4.881
LEU630
3.649
ILE639
4.617
ALA640
3.072
ASP641
3.002
PHE642
3.416
Ligand Name: 3-[4-(1-Formylpiperazin-4-yl)-benzylidenyl]-2-indolinone Ligand Info
Structure Description CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF FIBROBLAST GROWTH FACTOR RECEPTOR 1 IN COMPLEX WITH SU4984 INHIBITOR PDB:1AGW
Method X-ray diffraction Resolution 2.40 Å Mutation Yes [11]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGQVVLAEAI
498
GLPNRVTKVA
512
VKMLKSDATE
522

KDLSDLISEM
532
EMMKMIGKHK
542
NIINLLGACT
552
QDGPLYVIVE
562
YASKGNLREY
572

LQARRPPEEQ
594
LSSKDLVSCA
604
YQVARGMEYL
614
ASKKCIHRDL
624
AARNVLVTED
634

NVMKIADFGL
644
ARDIHHIDYY
654
KKTTNGRLPV
664
KWMAPEALFD
674
RIYTHQSDVW
684

SFGVLLWEIF
694
TLGGSPYPGV
704
PVEELFKLLK
714
EGHRMDKPSN
724
CTNELYMMMR
734

DCWHAVPSQR
744
PTFKQLVEDL
754
DRIVALTS
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SU2 or .SU22 or .SU23 or :3SU2;style chemicals stick;color identity;select .A:484 or .A:492 or .A:512 or .A:514 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:630 or .A:640 or .A:641; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.651
VAL492
4.142
ALA512
3.538
LYS514
4.486
ILE545
3.699
VAL561
3.508
GLU562
2.931
TYR563
3.115
Residue
Distance (Å)
ALA564
2.757
SER565
2.908
LYS566
3.552
GLY567
3.306
LEU630
3.539
ALA640
4.788
ASP641
4.673
Ligand Name: [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl 3-fluorosulfonylbenzoate Ligand Info
Structure Description Human FGF in complex with a covalent inhibitor PDB:5O49
Method X-ray diffraction Resolution 1.91 Å Mutation Yes [24]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKD
503
KPNRVTKVAV
513

KMLKSDATEK
523
DLSDLISEME
533
MMKMIGKHKN
543
IINLLGACTQ
553
DGPLYVIVEY
563

ASKGNLREYL
573
QARRPPEEQL
595
SSKDLVSCAY
605
QVARGMEYLA
615
SKKCIHRDLA
625

ARNVLVTEDN
635
VMKIADFGLA
645
RDIHHIDYYK
655
KTTNGRLPVK
665
WMAPEALFDR
675

IYTHQSDVWS
685
FGVLLWEIFT
695
LGGSPYPGVP
705
VEELFKLLKE
715
GHRMDKPSNC
725

TNELYMMMRD
735
CWHAVPSQRP
745
TFKQLVEDLD
755
RIVALTSNQ
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .9K5 or .9K52 or .9K53 or :39K5;style chemicals stick;color identity;select .A:484 or .A:485 or .A:486 or .A:487 or .A:488 or .A:489 or .A:490 or .A:491 or .A:492 or .A:512 or .A:514 or .A:531 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:568 or .A:630 or .A:641 or .A:644; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.157
GLY485
3.559
GLU486
3.000
GLY487
2.800
ALA488
4.159
PHE489
3.387
GLY490
3.280
GLN491
4.245
VAL492
3.358
ALA512
3.521
LYS514
1.682
Residue
Distance (Å)
GLU531
4.354
ILE545
4.135
VAL561
3.681
GLU562
2.734
TYR563
3.661
ALA564
3.024
ASN568
4.961
LEU630
3.674
ASP641
3.370
LEU644
4.279
Ligand Name: 3,4-dimethoxy-N-(5-phenyl-1H-pyrazol-3-yl)benzamide Ligand Info
Structure Description Fibroblast growth factor receptor 1 kinase in complex with JK-P3 PDB:4UWC
Method X-ray diffraction Resolution 1.96 Å Mutation Yes [12]
PDB Sequence
LPEDPRWELP
474
RDRLVLGKPL
484
GEGAFGQVVL
494
AEAIGLDKDK
504
PNRVTKVAVK
514

MLKSDATEKD
524
LSDLISEMEM
534
MKMIGKHKNI
544
INLLGACTQD
554
GPLYVIVEYA
564

SKGNLREYLQ
574
ARRPPGLEYS
584
YNPSHNPEEQ
594
LSSKDLVSCA
604
YQVARGMEYL
614

ASKKCIHRDL
624
AARNVLVTED
634
NVMKIADFGL
644
ARDIHHIDYY
654
KKTTNGRLPV
664

KWMAPEALFD
674
RIYTHQSDVW
684
SFGVLLWEIF
694
TLGGSPYPGV
704
PVEELFKLLK
714

EGHRMDKPSN
724
CTNELYMMMR
734
DCWHAVPSQR
744
PTFKQLVEDL
754
DRIVALTSNQ
764

E
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .4Y0 or .4Y02 or .4Y03 or :34Y0;style chemicals stick;color identity;select .A:484 or .A:489 or .A:492 or .A:512 or .A:514 or .A:531 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:571 or .A:630 or .A:640 or .A:641; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.689
PHE489
3.179
VAL492
2.918
ALA512
3.721
LYS514
3.075
GLU531
4.243
ILE545
2.981
VAL561
3.692
GLU562
2.007
Residue
Distance (Å)
TYR563
2.952
ALA564
2.076
SER565
2.284
LYS566
3.878
GLY567
3.630
GLU571
2.934
LEU630
3.032
ALA640
4.053
ASP641
4.466
Ligand Name: [(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl 4-ethyl-3-fluorosulfonyl-benzoate Ligand Info
Structure Description Human FGF in complex with a covalent inhibitor PDB:5O4A
Method X-ray diffraction Resolution 2.01 Å Mutation No [24]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKD
503
KPNRVTKVAV
513

KMLKSDATEK
523
DLSDLISEME
533
MMKMIGKHKN
543
IINLLGACTQ
553
DGPLYVIVEY
563

ASKGNLREYL
573
QARRPPGEEQ
594
LSSKDLVSCA
604
YQVARGMEYL
614
ASKKCIHRDL
624

AARNVLVTED
634
NVMKIADFGL
644
ARDIHHIDYY
654
KKTTNGRLPV
664
KWMAPEALFD
674

RIYTHQSDVW
684
SFGVLLWEIF
694
TLGGSPYPGV
704
PVEELFKLLK
714
EGHRMDKPSN
724

CTNELYMMMR
734
DCWHAVPSQR
744
PTFKQLVEDL
754
DRIVALTSNQ
764
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .9K8 or .9K82 or .9K83 or :39K8;style chemicals stick;color identity;select .A:484 or .A:485 or .A:486 or .A:487 or .A:489 or .A:490 or .A:491 or .A:492 or .A:512 or .A:514 or .A:531 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:568 or .A:630 or .A:641 or .A:644; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.241
GLY485
3.052
GLU486
3.487
GLY487
4.380
PHE489
3.137
GLY490
3.011
GLN491
4.317
VAL492
3.954
ALA512
3.496
LYS514
1.702
Residue
Distance (Å)
GLU531
4.496
ILE545
4.372
VAL561
3.893
GLU562
2.768
TYR563
3.701
ALA564
3.171
ASN568
4.762
LEU630
3.618
ASP641
3.169
LEU644
4.772
Ligand Name: 5-Bromo-N~4~-[3-(3-Methoxypropyl)-1h-Pyrazol-5-Yl]-N~2~-[(3-Methyl-1,2-Oxazol-5-Yl)methyl]pyrimidine-2,4-Diamine Ligand Info
Structure Description Crystal structure of Human Fibroblast Growth Factor Receptor 1 Kinase domain in complex with compound 6 PDB:4F64
Method X-ray diffraction Resolution 2.05 Å Mutation Yes [25]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGQVVLAEAI
498
GLPNRVTKVA
512
VKMLKSDATE
522

KDLSDLISEM
532
EMMKMIGKHK
542
NIINLLGACT
552
QDGPLYVIVE
562
YASKGNLREY
572

LQARRPPEEQ
594
LSSKDLVSCA
604
YQVARGMEYL
614
ASKKCIHRDL
624
AARNVLVTED
634

NVMKIADFGL
644
ARDIHHIDYY
654
KKTTNGRLPV
664
KWMAPEALFD
674
RIYTHQSDVW
684

SFGVLLWEIF
694
TLGGSPYPGV
704
PVEELFKLLK
714
EGHRMDKPSN
724
CTNELYMMMR
734

DCWHAVPSQR
744
PTFKQLVEDL
754
DRIVALTS
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .0S8 or .0S82 or .0S83 or :30S8;style chemicals stick;color identity;select .A:484 or .A:485 or .A:492 or .A:512 or .A:514 or .A:531 or .A:535 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:627 or .A:628 or .A:630 or .A:640 or .A:641; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.010
GLY485
4.076
VAL492
3.852
ALA512
3.388
LYS514
3.626
GLU531
4.170
MET535
4.808
ILE545
4.202
VAL561
3.554
GLU562
2.895
Residue
Distance (Å)
TYR563
3.779
ALA564
3.018
SER565
3.501
LYS566
4.562
GLY567
3.592
ARG627
3.664
ASN628
4.316
LEU630
3.579
ALA640
4.124
ASP641
4.204
Ligand Name: N~4~-{3-[2-(3,4-Dimethoxyphenyl)ethyl]-1h-Pyrazol-5-Yl}-N~2~-[(3-Methyl-1,2-Oxazol-5-Yl)methyl]pyrimidine-2,4-Diamine Ligand Info
Structure Description Crystal structure of human fibroblast growth factor receptor 1 kinase domain in complex with pyrazolaminopyrimidine 2 PDB:4NKA
Method X-ray diffraction Resolution 2.19 Å Mutation Yes [26]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEQVVLAEA
497
IGLDKDKPNR
507
VTKVAVKMLK
517

SDATEKDLSD
527
LISEMEMMKM
537
IGKHKNIINL
547
LGACTQDGPL
557
YVIVEYASKG
567

NLREYLQARR
577
PPEEQLSSKD
599
LVSCAYQVAR
609
GMEYLASKKC
619
IHRDLAARNV
629

LVTEDNVMKI
639
ADFGIDYYKK
656
TTNGRLPVKW
666
MAPEALFDRI
676
YTHQSDVWSF
686

GVLLWEIFTL
696
GGSPYPGVPV
706
EELFKLLKEG
716
HRMDKPSNCT
726
NELYMMMRDC
736

WHAVPSQRPT
746
FKQLVEDLDR
756
IVALTSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .2K7 or .2K72 or .2K73 or :32K7;style chemicals stick;color identity;select .A:484 or .A:485 or .A:492 or .A:512 or .A:514 or .A:528 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:567 or .A:627 or .A:628 or .A:630 or .A:640 or .A:641; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.229
GLY485
4.000
VAL492
4.022
ALA512
3.490
LYS514
4.268
LEU528
4.459
GLU531
3.073
MET535
4.581
ILE545
3.799
VAL559
4.864
VAL561
3.724
Residue
Distance (Å)
GLU562
2.822
TYR563
3.500
ALA564
2.791
SER565
4.775
GLY567
3.626
ARG627
3.657
ASN628
4.338
LEU630
3.626
ALA640
4.011
ASP641
3.393
Ligand Name: N-[2-[[6-[(2,6-dichloro-3,5-dimethoxyphenyl)carbamoyl-methylamino]pyrimidin-4-yl]amino]-5-(4-ethylpiperazin-1-yl)phenyl]propanamide Ligand Info
Structure Description Crystal structure of FGFR1-Y563C (FGFR4 surrogate) covalently bound to H3B-6527 PDB:5VND
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [27]
PDB Sequence
YELPEDPRWE
472
LPRDRLVLGK
482
PLGEGAFGQV
492
VLAEAIGLDK
502
DKPNRVTKVA
512

VKMLKSDATE
522
KDLSDLISEM
532
EMMKMIGKHK
542
NIINLLGACT
552
QDGPLYVIVE
562

CASKGNLREY
572
LQARRPPGLE
582
YSYNPSHNPE
592
EQLSSKDLVS
602
CAYQVARGME
612

YLASKKCIHR
622
DLAARNVLVT
632
EDNVMKIADF
642
GLARDHHIDY
653
YKKTTNGRLP
663

VKWMAPEALF
673
DRIYTHQSDV
683
WSFGVLLWEI
693
FTLGGSPYPG
703
VPVEELFKLL
713

KEGHRMDKPS
723
NCTNELYMMM
733
RDCWHAVPSQ
743
RPTFKQLVED
753
LDRIVALTSN
763

QE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .9ES or .9ES2 or .9ES3 or :39ES;style chemicals stick;color identity;select .A:484 or .A:489 or .A:492 or .A:494 or .A:511 or .A:512 or .A:513 or .A:514 or .A:528 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:567 or .A:568 or .A:571 or .A:630 or .A:640 or .A:641 or .A:642 or .A:643; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.923
PHE489
4.931
VAL492
3.378
LEU494
3.356
VAL511
4.345
ALA512
3.637
VAL513
4.174
LYS514
3.308
LEU528
4.749
GLU531
3.393
MET535
3.918
ILE545
3.816
VAL559
3.601
Residue
Distance (Å)
VAL561
3.637
GLU562
3.203
CYS563
1.594
ALA564
2.749
SER565
4.338
GLY567
3.471
ASN568
4.145
GLU571
3.350
LEU630
3.731
ALA640
3.262
ASP641
3.106
PHE642
3.796
GLY643
4.340
Ligand Name: N-[2-[[6-[(2,6-dichloro-3,5-dimethoxyphenyl)carbamoyl-[3-(4-methylpiperazin-1-yl)propyl]amino]pyrimidin-4-yl]amino]phenyl]prop-2-enamide Ligand Info
Structure Description Crystal structure of FGFR1-Y563C (FGFR4 surrogate) covalently bound to compound 11. PDB:6P69
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [28]
PDB Sequence
EYELPEDPRW
471
ELPRDRLVLG
481
KPLGEGAFGQ
491
VVLAEAIGLP
505
NRVTKVAVKM
515

LKSDATEKDL
525
SDLISEMEMM
535
KMIGKHKNII
545
NLLGACTQDG
555
PLYVIVECAS
565

KGNLREYLQA
575
RRPPEEQLSS
597
KDLVSCAYQV
607
ARGMEYLASK
617
KCIHRDLAAR
627

NVLVTEDNVM
637
KIADFGLARD
647
IHHIDYYKKT
657
TNGRLPVKWM
667
APEALFDRIY
677

THQSDVWSFG
687
VLLWEIFTLG
697
GSPYPGVPVE
707
ELFKLLKEGH
717
RMDKPSNCTN
727

ELYMMMRDCW
737
HAVPSQRPTF
747
KQLVEDLDRI
757
VALTSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .O21 or .O212 or .O213 or :3O21;style chemicals stick;color identity;select .A:484 or .A:485 or .A:486 or .A:487 or .A:492 or .A:494 or .A:510 or .A:512 or .A:513 or .A:514 or .A:528 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:630 or .A:640 or .A:641 or .A:642 or .A:643; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.240
GLY485
4.280
GLU486
3.260
GLY487
3.226
VAL492
3.509
LEU494
3.184
LYS510
4.171
ALA512
3.645
VAL513
3.956
LYS514
3.519
LEU528
4.922
GLU531
3.390
MET535
3.807
Residue
Distance (Å)
ILE545
3.758
VAL559
3.686
VAL561
3.542
GLU562
3.083
CYS563
1.612
ALA564
2.785
SER565
3.812
LEU630
3.604
ALA640
3.250
ASP641
2.985
PHE642
3.799
GLY643
4.508
Ligand Name: 5-Bromo-N~2~-[(3-Methyl-1,2-Oxazol-5-Yl)methyl]-N~4~-[3-(2-Phenylethyl)-1h-Pyrazol-5-Yl]pyrimidine-2,4-Diamine Ligand Info
Structure Description Crystal structure of Human Fibroblast Growth Factor Receptor 1 Kinase domain in complex with compound 8 PDB:4F65
Method X-ray diffraction Resolution 2.26 Å Mutation Yes [25]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKP
505
NRVTKVAVKM
515

LKSDATEKDL
525
SDLISEMEMM
535
KMIGKHKNII
545
NLLGACTQDG
555
PLYVIVEYAS
565

KGNLREYLQA
575
RRPPPEEQLS
596
SKDLVSCAYQ
606
VARGMEYLAS
616
KKCIHRDLAA
626

RNVLVTEDNV
636
MKIADFYYKK
656
TTNGRLPVKW
666
MAPEALFDRI
676
YTHQSDVWSF
686

GVLLWEIFTL
696
GGSPYPGVPV
706
EELFKLLKEG
716
HRMDKPSNCT
726
NELYMMMRDC
736

WHAVPSQRPT
746
FKQLVEDLDR
756
IVALTSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .0S9 or .0S92 or .0S93 or :30S9;style chemicals stick;color identity;select .A:484 or .A:485 or .A:486 or .A:487 or .A:488 or .A:492 or .A:512 or .A:514 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:627 or .A:628 or .A:630 or .A:640 or .A:641; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.060
GLY485
3.755
GLU486
3.472
GLY487
3.530
ALA488
4.805
VAL492
3.580
ALA512
3.314
LYS514
3.402
GLU531
3.535
MET535
4.157
ILE545
4.126
VAL559
4.549
Residue
Distance (Å)
VAL561
3.439
GLU562
2.910
TYR563
3.664
ALA564
2.819
SER565
3.377
LYS566
4.406
GLY567
3.556
ARG627
3.632
ASN628
4.453
LEU630
3.583
ALA640
4.144
ASP641
4.000
Ligand Name: N-[4-(4-methylpiperazin-1-yl)phenyl]-1H-indazole-3-carboxamide Ligand Info
Structure Description Fibroblast growth factor receptor 1 kinase in complex with JK-P5 PDB:4UWB
Method X-ray diffraction Resolution 2.31 Å Mutation Yes [12]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKD
503
KPNRVTKVAV
513

KMLKSDATEK
523
DLSDLISEME
533
MMKMIGKHKN
543
IINLLGACTQ
553
DGPLYVIVEY
563

ASKGNLREYL
573
QARRPPGLEY
583
SPSHNPEEQL
595
SSKDLVSCAY
605
QVARGMEYLA
615

SKKCIHRDLA
625
ARNVLVTEDN
635
VMKIADFGLA
645
RDHHIDYYKK
656
TTNGRLPVKW
666

MAPEALFDRI
676
YTHQSDVWSF
686
GVLLWEIFTL
696
GGSPYPGVPV
706
EELFKLLKEG
716

HRMDKPSNCT
726
NELYMMMRDC
736
WHAVPSQRPT
746
FKQLVEDLDR
756
IVALTSNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .JVT or .JVT2 or .JVT3 or :3JVT;style chemicals stick;color identity;select .A:484 or .A:492 or .A:512 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:571 or .A:630; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.456
VAL492
3.949
ALA512
3.520
ILE545
3.890
VAL561
3.469
GLU562
2.825
TYR563
3.857
Residue
Distance (Å)
ALA564
2.858
SER565
3.502
LYS566
4.209
GLY567
3.452
GLU571
4.200
LEU630
3.492
Ligand Name: N~2~-[(3-Methyl-1,2-Oxazol-5-Yl)methyl]-N~4~-[5-(2-Phenylethyl)-1h-Pyrazol-3-Yl]pyrimidine-2,4-Diamine Ligand Info
Structure Description Crystal structure of human fibroblast growth factor receptor 1 kinase domain in complex with pyrazolaminopyrimidine 3 PDB:4NKS
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [26]
PDB Sequence
LPEDPRWELP
474
RDRLVLGKPL
484
GQVVLAEAIN
506
RVTKVAVKML
516
KDATEKDLSD
527

LISEMEMMKM
537
IGKHKNIINL
547
LGACTQDGPL
557
YVIVEYASKG
567
NLREYLQARR
577

PPQLSSKDLV
601
SCAYQVARGM
611
EYLASKKCIH
621
RDLAARNVLV
631
TEDNVMKIAD
641

FGLIDYYKKT
657
TNGRLPVKWM
667
APEALFDRIY
677
THQSDVWSFG
687
VLLWEIFTLG
697

GSPYPGVPVE
707
ELFKLLKEGH
717
RMDKPSNCTN
727
ELYMMMRDCW
737
HAVPSQRPTF
747

KQLVEDLDRI
757
VALTS
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .2M2 or .2M22 or .2M23 or :32M2;style chemicals stick;color identity;select .A:484 or .A:485 or .A:492 or .A:512 or .A:513 or .A:514 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:567 or .A:627 or .A:628 or .A:630 or .A:640 or .A:641; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.543
GLY485
4.255
VAL492
3.901
ALA512
3.706
VAL513
4.582
LYS514
3.292
GLU531
3.578
MET535
3.839
ILE545
4.138
VAL559
4.058
Residue
Distance (Å)
VAL561
3.324
GLU562
2.877
TYR563
3.657
ALA564
2.979
GLY567
4.002
ARG627
4.021
ASN628
4.519
LEU630
3.557
ALA640
3.890
ASP641
4.555
Ligand Name: 5-Bromo-N~4~-(3-Methyl-1h-Pyrazol-5-Yl)-N~2~-[2-(Pyridin-3-Yl)ethyl]pyrimidine-2,4-Diamine Ligand Info
Structure Description Crystal structure of Human Fibroblast Growth Factor Receptor 1 Kinase domain in complex with compound 1 PDB:4F63
Method X-ray diffraction Resolution 2.55 Å Mutation Yes [25]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGQVVLAEAI
498
GLPNRVTKVA
512
VKMLKSDATE
522

KDLSDLISEM
532
EMMKMIGKHK
542
NIINLLGACT
552
QDGPLYVIVE
562
YASKGNLREY
572

LQARRPPEEQ
594
LSSKDLVSCA
604
YQVARGMEYL
614
ASKKCIHRDL
624
AARNVLVTED
634

NVMKIADFGL
644
ARDIHHIDYY
654
KKTTNGRLPV
664
KWMAPEALFD
674
RIYTHQSDVW
684

SFGVLLWEIF
694
TLGGSPYPGV
704
PVEELFKLLK
714
EGHRMDKPSN
724
CTNELYMMMR
734

DCWHAVPSQR
744
PTFKQLVEDL
754
DRIVALTS
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .0S7 or .0S72 or .0S73 or :30S7;style chemicals stick;color identity;select .A:484 or .A:485 or .A:492 or .A:512 or .A:514 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:630 or .A:640 or .A:641; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
2.919
GLY485
3.507
VAL492
3.370
ALA512
3.600
LYS514
4.336
ILE545
4.433
VAL561
3.528
GLU562
2.856
Residue
Distance (Å)
TYR563
3.513
ALA564
2.776
SER565
3.262
LYS566
4.296
GLY567
3.612
LEU630
3.722
ALA640
4.238
ASP641
3.220
Ligand Name: N~4~-{5-[2-(3,5-Dimethoxyphenyl)ethyl]-1h-Pyrazol-3-Yl}-N~2~-[(3-Methyl-1,2-Oxazol-5-Yl)methyl]pyrimidine-2,4-Diamine Ligand Info
Structure Description Crystal structure of human fibroblast growth factor receptor 1 kinase domain in complex with pyrazolaminopyrimidine 1 PDB:4NK9
Method X-ray diffraction Resolution 2.57 Å Mutation Yes [26]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDDK
504
PNRVTKVAVK
514

MLKSDATEKD
524
LSDLISEMEM
534
MKMIGKHKNI
544
INLLGACTQD
554
GPLYVIVEYA
564

SKGNLREYLQ
574
ARRPPEQLSS
597
KDLVSCAYQV
607
ARGMEYLASK
617
KCIHRDLAAR
627

NVLVTEDNVM
637
KIADFGIDYY
654
KKTTNGRLPV
664
KWMAPEALFD
674
RIYTHQSDVW
684

SFGVLLWEIF
694
TLGGSPYPGV
704
PVEELFKLLK
714
EGHRMDKPSN
724
CTNELYMMMR
734

DCWHAVPSQR
744
PTFKQLVEDL
754
DRIVALTSNQ
764
E
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .2K5 or .2K52 or .2K53 or :32K5;style chemicals stick;color identity;select .A:484 or .A:485 or .A:486 or .A:487 or .A:488 or .A:492 or .A:512 or .A:514 or .A:528 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:567 or .A:568 or .A:627 or .A:628 or .A:630 or .A:639 or .A:640 or .A:641 or .A:642; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
2.930
GLY485
3.640
GLU486
3.471
GLY487
3.241
ALA488
4.592
VAL492
3.479
ALA512
3.552
LYS514
3.325
LEU528
4.408
GLU531
3.574
MET535
4.021
ILE545
3.503
VAL559
3.763
VAL561
3.644
Residue
Distance (Å)
GLU562
3.039
TYR563
3.863
ALA564
2.784
SER565
4.935
GLY567
3.503
ASN568
4.944
ARG627
4.523
ASN628
4.913
LEU630
3.484
ILE639
4.545
ALA640
3.724
ASP641
3.209
PHE642
3.621
Ligand Name: N-[2-[[5-[(2,6-dichloro-3,5-dimethoxyphenyl)methoxy]pyrimidin-2-yl]amino]-3-methylphenyl]propanamide Ligand Info
Structure Description FGFR1 complex with N-(2-((5-((2,6-dichloro-3,5-dimethoxybenzyl)oxy)pyrimidin-2-yl)amino)-3-methylphenyl)acrylamide PDB:6NVL
Method X-ray diffraction Resolution 2.70 Å Mutation Yes [29]
PDB Sequence
YELPEDPRWE
472
LPRDRLVLGK
482
PLGEGCFGQV
492
VLAEAIGLDK
502
DKPNRVTKVA
512

VKMLKSDATE
522
KDLSDLISEM
532
EMMKMIGKHK
542
NIINLLGACT
552
QDGPLYVIVE
562

YASKGNLREY
572
LQARRPPQLS
596
SKDLVSCAYQ
606
VARGMEYLAS
616
KKCIHRDLAA
626

RNVLVTEDNV
636
MKIADFGLYY
654
KKTNGRLPVK
665
WMAPEALFDR
675
IYTHQSDVWS
685

FGVLLWEIFT
695
LGGSPYPGVP
705
VEELFKLLKE
715
GHRMDKPSNC
725
TNELYMMMRD
735

CWHAVPSQRP
745
TFKQLVEDLD
755
RIVALTSNQE
765
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .XL6 or .XL62 or .XL63 or :3XL6;style chemicals stick;color identity;select .A:484 or .A:487 or .A:488 or .A:492 or .A:494 or .A:512 or .A:513 or .A:514 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:568 or .A:571 or .A:627 or .A:630 or .A:639 or .A:640 or .A:641 or .A:642; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.638
GLY487
3.162
CYS488
1.828
VAL492
3.906
LEU494
4.268
ALA512
3.280
VAL513
3.958
LYS514
3.665
GLU531
3.462
MET535
3.332
ILE545
3.853
VAL559
4.051
VAL561
3.371
GLU562
3.514
Residue
Distance (Å)
TYR563
3.507
ALA564
2.924
SER565
3.838
LYS566
4.996
GLY567
3.669
ASN568
3.389
GLU571
4.341
ARG627
4.998
LEU630
3.519
ILE639
4.676
ALA640
3.135
ASP641
3.028
PHE642
3.573
Ligand Name: N-[3-[[6-[(2,6-dichloro-3,5-dimethoxyphenyl)carbamoyl-methylamino]pyrimidin-4-yl]amino]-1-(2-hydroxyethyl)pyrazol-4-yl]prop-2-enamide Ligand Info
Structure Description Crystal structure of FGFR1-Y563C (FGFR4 surrogate) covalently bound to compound 22. PDB:6P68
Method X-ray diffraction Resolution 2.90 Å Mutation Yes [30]
PDB Sequence
EYELPEDPRW
471
ELPRDRLVLG
481
KPLGEGAFGQ
491
VVLAEAIGLD
501
KDKPNRVTKV
511

AVKMLKSDAT
521
EKDLSDLISE
531
MEMMKMIGKH
541
KNIINLLGAC
551
TQDGPLYVIV
561

ECASKGNLRE
571
YLQARRPPEE
593
QLSSKDLVSC
603
AYQVARGMEY
613
LASKKCIHRD
623

LAARNVLVTE
633
DNVMKIADFG
643
LARDIDYYKK
656
TTNGRLPVKW
666
MAPEALFDRI
676

YTHQSDVWSF
686
GVLLWEIFTL
696
GGSPYPGVPV
706
EELFKLLKEG
716
HRMDKPSNCT
726

NELYMMMRDC
736
WHAVPSQRPT
746
FKQLVEDLDR
756
IVALTSN
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .O1Y or .O1Y2 or .O1Y3 or :3O1Y;style chemicals stick;color identity;select .A:484 or .A:492 or .A:494 or .A:510 or .A:512 or .A:513 or .A:514 or .A:528 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:567 or .A:568 or .A:571 or .A:630 or .A:640 or .A:641 or .A:642 or .A:643; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.451
VAL492
3.842
LEU494
3.675
LYS510
4.690
ALA512
3.628
VAL513
4.574
LYS514
3.652
LEU528
4.991
GLU531
3.258
MET535
3.306
ILE545
3.921
VAL559
3.805
VAL561
3.754
Residue
Distance (Å)
GLU562
2.794
CYS563
1.745
ALA564
2.912
SER565
4.232
GLY567
4.138
ASN568
4.718
GLU571
3.222
LEU630
3.500
ALA640
3.197
ASP641
2.830
PHE642
3.631
GLY643
4.796
Ligand Name: 4-azanyl-3-(3,5-dimethyl-1-benzofuran-2-yl)-2-phenyl-6~{H}-pyrazolo[3,4-d]pyridazin-7-one Ligand Info
Structure Description Crystal structure of FGFR1 kinase domain in complex with compound 3 PDB:6ITJ
Method X-ray diffraction Resolution 1.99 Å Mutation Yes [31]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKD
503
KPNRVTKVAV
513

KMLKSDATEK
523
DLSDLISEME
533
MMKMIGKHKN
543
IINLLGACTQ
553
DGPLYVIVEY
563

ASKGNLREYL
573
QARRPPEEQL
595
SSKDLVSCAY
605
QVARGMEYLA
615
SKKCIHRDLA
625

ARNVLVTEDN
635
VMKIADFGLA
645
RDIHHIDYYK
655
KTTNGRLPVK
665
WMAPEALFDR
675

IYTHQSDVWS
685
FGVLLWEIFT
695
LGGSPYPGVP
705
VEELFKLLKE
715
GHRMDKPSNC
725

TNELYMMMRD
735
CWHAVPSQRP
745
TFKQLVEDLD
755
RIVALTSNQE
765
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .AXU or .AXU2 or .AXU3 or :3AXU;style chemicals stick;color identity;select .A:484 or .A:485 or .A:489 or .A:492 or .A:512 or .A:513 or .A:514 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:567 or .A:568 or .A:630 or .A:640 or .A:641; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.917
GLY485
4.498
PHE489
3.774
VAL492
3.304
ALA512
3.373
VAL513
4.006
LYS514
3.389
GLU531
3.092
MET535
4.589
ILE545
4.479
VAL559
3.734
Residue
Distance (Å)
VAL561
3.451
GLU562
2.971
TYR563
3.573
ALA564
2.702
SER565
4.731
GLY567
3.622
ASN568
4.850
LEU630
3.440
ALA640
4.147
ASP641
3.569
Ligand Name: 4-(4-Ethylpiperazin-1-Yl)-N-[6-(3-Methoxyphenyl)-2h-Indazol-3-Yl]benzamide Ligand Info
Structure Description Crystal structure of FGFR1 kinase domain in complex with 7n PDB:4ZSA
Method X-ray diffraction Resolution 2.00 Å Mutation Yes [32]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKD
503
KPNRVTKVAV
513

KMLKSDATEK
523
DLSDLISEME
533
MMKMIGKHKN
543
IINLLGACTQ
553
DGPLYVIVEY
563

ASKGNLREYL
573
QARRPPEEQL
595
SSKDLVSCAY
605
QVARGMEYLA
615
SKKCIHRDLA
625

ARNVLVTEDN
635
VMKIADFGLA
645
RDIHHIDYYK
655
KTTNGRLPVK
665
WMAPEALFDR
675

IYTHQSDVWS
685
FGVLLWEIFT
695
LGGSPYPGVP
705
VEELFKLLKE
715
GHRMDKPSNC
725

TNELYMMMRD
735
CWHAVPSQRP
745
TFKQLVEDLD
755
RIVALTSNQE
765
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .4UT or .4UT2 or .4UT3 or :34UT;style chemicals stick;color identity;select .A:484 or .A:485 or .A:489 or .A:492 or .A:512 or .A:514 or .A:528 or .A:531 or .A:535 or .A:545 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:568 or .A:571 or .A:630 or .A:640 or .A:641; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
3.524
GLY485
3.530
PHE489
3.573
VAL492
3.838
ALA512
3.471
LYS514
3.574
LEU528
4.847
GLU531
3.346
MET535
4.166
ILE545
4.188
VAL559
4.002
VAL561
3.656
Residue
Distance (Å)
GLU562
2.743
TYR563
3.569
ALA564
2.829
SER565
3.205
LYS566
4.126
GLY567
3.432
ASN568
4.923
GLU571
3.931
LEU630
3.380
ALA640
4.745
ASP641
3.941
Ligand Name: 1-[(6-chloroimidazo[1,2-b]pyridazin-3-yl)sulfonyl]-6-(1-methyl-1H-pyrazol-4-yl)-1H-pyrazolo[4,3-b]pyridine Ligand Info
Structure Description Crystal structure of FGFR1 kinase domain in complex with a novel inhibitor PDB:5Z0S
Method X-ray diffraction Resolution 2.45 Å Mutation Yes [33]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEGAFGQVV
493
LAEAIGLDKP
505
NRVTKVAVKM
515

LKSDATEKDL
525
SDLISEMEMM
535
KMIGKHKNII
545
NLLGACTQDG
555
PLYVIVEYAS
565

KGNLREYLQA
575
RRPPEEQLSS
597
KDLVSCAYQV
607
ARGMEYLASK
617
KCIHRDLAAR
627

NVLVTEDNVM
637
KIADFGLARD
647
IHHIDYYKKT
657
TNGRLPVKWM
667
APEALFDRIY
677

THQSDVWSFG
687
VLLWEIFTLG
697
GSPYPGVPVE
707
ELFKLLKEGH
717
RMDKPSNCTN
727

ELYMMMRDCW
737
HAVPSQRPTF
747
KQLVEDLDRI
757
VALTS
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .960 or .9602 or .9603 or :3960;style chemicals stick;color identity;select .A:484 or .A:485 or .A:489 or .A:492 or .A:512 or .A:514 or .A:531 or .A:545 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:567 or .A:568 or .A:571 or .A:627 or .A:628 or .A:630 or .A:640 or .A:641; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
2.899
GLY485
3.144
PHE489
3.132
VAL492
3.927
ALA512
3.637
LYS514
3.663
GLU531
4.354
ILE545
3.344
VAL561
3.383
GLU562
3.355
TYR563
3.416
Residue
Distance (Å)
ALA564
2.768
SER565
4.800
GLY567
4.539
ASN568
3.474
GLU571
4.693
ARG627
2.908
ASN628
3.754
LEU630
3.452
ALA640
3.871
ASP641
3.227
Ligand Name: 1-Tert-Butyl-3-[2-[3-(Diethylamino)propylamino]-6-(3,5-Dimethoxyphenyl)pyrido[2,3-D]pyrimidin-7-Yl]urea Ligand Info
Structure Description FGFR1 ligand complex PDB:5A4C
Method X-ray diffraction Resolution 2.09 Å Mutation Yes [34]
PDB Sequence
ELPEDPRWEL
473
PRDRLVLGKP
483
LGEFGQVVLA
495
EAIGLDKDKP
505
NRVTKVAVKM
515

LKSDATEKDL
525
SDLISEMEMM
535
KMIGKHKNII
545
NLLGACTQDG
555
PLYVIVEYAS
565

KGNLREYLQA
575
RRPPGLEYSY
585
NPSHNPEEQL
595
SSKDLVSCAY
605
QVARGMEYLA
615

SKKCIHRDLA
625
ARNVLVTEDN
635
VMKIADFGLI
651
DYYKKTTNGR
661
LPVKWMAPEA
671

LFDRIYTHQS
681
DVWSFGVLLW
691
EIFTLGGSPY
701
PGVPVEELFK
711
LLKEGHRMDK
721

PSNCTNELYM
731
MMRDCWHAVP
741
SQRPTFKQLV
751
EDLDRIVALT
761
SNQE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .XOJ or .XOJ2 or .XOJ3 or :3XOJ;style chemicals stick;color identity;select .A:482 or .A:484 or .A:485 or .A:486 or .A:490 or .A:491 or .A:492 or .A:512 or .A:514 or .A:528 or .A:531 or .A:535 or .A:545 or .A:547 or .A:559 or .A:561 or .A:562 or .A:563 or .A:564 or .A:565 or .A:566 or .A:567 or .A:568 or .A:571 or .A:630 or .A:639 or .A:640 or .A:641 or .A:642 or .A:643; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS482
2.795
LEU484
2.640
GLY485
2.832
GLU486
2.927
GLY490
4.246
GLN491
4.806
VAL492
3.413
ALA512
3.606
LYS514
3.398
LEU528
4.074
GLU531
2.725
MET535
2.897
ILE545
3.239
LEU547
4.917
VAL559
2.971
Residue
Distance (Å)
VAL561
2.941
GLU562
2.374
TYR563
2.714
ALA564
1.988
SER565
2.642
LYS566
3.180
GLY567
2.767
ASN568
4.787
GLU571
3.418
LEU630
3.421
ILE639
4.142
ALA640
3.184
ASP641
2.833
PHE642
2.782
GLY643
4.832
Ligand Name: (6s)-6-Phenyl-5,6-Dihydrobenzo[h]quinazolin-2-Amine Ligand Info
Structure Description Crystal structure of the catalytic domain of FGFR1 kinase in complex with ARQ 069 PDB:3RHX
Method X-ray diffraction Resolution 2.01 Å Mutation Yes [35]
PDB Sequence
SEYELPEDPR
470
WELPRDRLVL
480
GKPLGEGAFG
490
QVVLAEAIGL
500
PNRVTKVAVK
514

MLKSDATEKD
524
LSDLISEMEM
534
MKMIGKHKNI
544
INLLGACTQD
554
GPLYVIVEYA
564

SKGNLREYLQ
574
ARRQLSSKDL
600
VSCAYQVARG
610
MEYLASKKCI
620
HRDLAARNVL
630

VTEDNVMKIA
640
DFGLADYYKK
656
TTNGRLPVKW
666
MAPEALFDRI
676
YTHQSDVWSF
686

GVLLWEIFTL
696
GGSPYPGVPV
706
EELFKLLKEG
716
HRMDKPSNCT
726
NELYMMMRDC
736

WHAVPSQRPT
746
FKQLVEDLDR
756
IVALT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .3RH or .3RH2 or .3RH3 or :33RH;style chemicals stick;color identity;select .B:484 or .B:485 or .B:489 or .B:492 or .B:512 or .B:514 or .B:531 or .B:535 or .B:545 or .B:561 or .B:562 or .B:563 or .B:564 or .B:565 or .B:630 or .B:640 or .B:641; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU484
4.094
GLY485
4.351
PHE489
3.977
VAL492
3.727
ALA512
3.665
LYS514
4.052
GLU531
3.190
MET535
3.934
ILE545
3.649
Residue
Distance (Å)
VAL561
3.659
GLU562
3.148
TYR563
3.661
ALA564
2.863
SER565
4.984
LEU630
3.360
ALA640
3.777
ASP641
3.677
References  Top
REF 1 Characterization of the cholangiocarcinoma drug pemigatinib against FGFR gatekeeper mutants. Commun Chem. 2022 Aug 22;5(1):100.
REF 2 Landscape of activating cancer mutations in FGFR kinases and their differential responses to inhibitors in clinical use. Oncotarget. 2016 Apr 26;7(17):24252-68.
REF 3 Lenvatinib inhibits angiogenesis and tumor fibroblast growth factor signaling pathways in human hepatocellular carcinoma models. Cancer Med. 2018 Jun;7(6):2641-2653.
REF 4 Discovery of 3-(2,6-dichloro-3,5-dimethoxy-phenyl)-1-{6-[4-(4-ethyl-piperazin-1-yl)-phenylamino]-pyrimidin-4-yl}-1-methyl-urea (NVP-BGJ398), a potent and selective inhibitor of the fibroblast growth factor receptor family of receptor tyrosine kinase. J Med Chem. 2011 Oct 27;54(20):7066-83.
REF 5 The 1.65?? resolution structure of the complex of AZD4547 with the kinase domain of FGFR1 displays exquisite molecular recognition. Acta Crystallogr D Biol Crystallogr. 2015 Mar;71(Pt 3):525-33.
REF 6 TAS-120 Cancer Target Binding: Defining Reactivity and Revealing the First Fibroblast Growth Factor Receptor?1 (FGFR1) Irreversible Structure. ChemMedChem. 2019 Feb 19;14(4):494-500.
REF 7 The Effect of Mutations on Drug Sensitivity and Kinase Activity of Fibroblast Growth Factor Receptors: A Combined Experimental and Theoretical Study. EBioMedicine. 2015 Mar 1;2(3):194-204.
REF 8 The fibroblast growth factor receptor genetic status as a potential predictor of the sensitivity to CH5183284/Debio 1347, a novel selective FGFR inhibitor. Mol Cancer Ther. 2014 Nov;13(11):2547-58.
REF 9 The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site. Cell. 2009 Aug 7;138(3):514-24.
REF 10 Crystal structure of an angiogenesis inhibitor bound to the FGF receptor tyrosine kinase domain. EMBO J. 1998 Oct 15;17(20):5896-904.
REF 11 Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors. Science. 1997 May 9;276(5314):955-60.
REF 12 Validation of ion mobility spectrometry - mass spectrometry as a screening tool to identify type II kinase inhibitors of FGFR1 kinase. Rapid Commun Mass Spectrom. 2021 May 26:e9130.
REF 13 Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent antimelanoma activity. Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3041-6.
REF 14 Pyrido[2,3-d]pyrimidin-5-ones: a novel class of antiinflammatory macrophage colony-stimulating factor-1 receptor inhibitors. J Med Chem. 2009 Feb 26;52(4):1081-99.
REF 15 Optimization of a potent class of arylamide colony-stimulating factor-1 receptor inhibitors leading to anti-inflammatory clinical candidate 4-cyano-N-[2-(1-cyclohexen-1-yl)-4-[1-[(dimethylamino)acetyl]-4-piperidinyl]phenyl]-1H-imidazole-2-carboxamide (JNJ-28312141). J Med Chem. 2011 Nov 24;54(22):7860-83.
REF 16 Discovery of novel fibroblast growth factor receptor 1 kinase inhibitors by structure-based virtual screening. J Med Chem. 2010 Feb 25;53(4):1662-72.
REF 17 Understanding the structural requirements for covalent inhibition of FGFR1-3
REF 18 Understanding the structural requirements for covalent inhibition of FGFR1-3
REF 19 Understanding the structural requirements for covalent inhibition of FGFR1-3
REF 20 2-Oxo-3, 4-dihydropyrimido[4, 5-d]pyrimidinyl derivatives as new irreversible pan fibroblast growth factor receptor (FGFR) inhibitors. Eur J Med Chem. 2017 Jul 28;135:531-543.
REF 21 A new class of FGFR1 inhibitors
REF 22 Fragment screening diverse active sites
REF 23 Understanding the structural requirements for covalent inhibition of FGFR1-3
REF 24 A study of the reactivity of S((VI))-F containing warheads with nucleophilic amino-acid side chains under physiological conditions. Org Biomol Chem. 2017 Nov 22;15(45):9685-9695.
REF 25 Protein-ligand crystal structures can guide the design of selective inhibitors of the FGFR tyrosine kinase. J Med Chem. 2012 Jun 14;55(11):5003-12.
REF 26 FGFR1 Kinase Inhibitors: Close Regioisomers Adopt Divergent Binding Modes and Display Distinct Biophysical Signatures. ACS Med Chem Lett. 2013 Dec 6;5(2):166-71.
REF 27 H3B-6527 Is a Potent and Selective Inhibitor of FGFR4 in FGF19-Driven Hepatocellular Carcinoma. Cancer Res. 2017 Dec 15;77(24):6999-7013.
REF 28 To be published
REF 29 Rotational Freedom, Steric Hindrance, and Protein Dynamics Explain BLU554 Selectivity for the Hinge Cysteine of FGFR4. ACS Med Chem Lett. 2019 Jul 3;10(8):1180-1186.
REF 30 To be published
REF 31 Discovery and Development of a Series of Pyrazolo[3,4-d]pyridazinone Compounds as the Novel Covalent Fibroblast Growth Factor Receptor Inhibitors by the Rational Drug Design. J Med Chem. 2019 Aug 22;62(16):7473-7488.
REF 32 Design, synthesis and biological evaluation of novel FGFR inhibitors bearing an indazole scaffold. Org Biomol Chem. 2015 Jul 28;13(28):7643-54.
REF 33 Structure-Based Discovery of a Series of 5H-Pyrrolo[2,3-b]pyrazine FGFR Kinase Inhibitors. Molecules. 2018 Mar 19;23(3):698.
REF 34 Structural and dynamic insights into the energetics of activation loop rearrangement in FGFR1 kinase. Nat Commun. 2015 Jul 23;6:7877.
REF 35 A novel mode of protein kinase inhibition exploiting hydrophobic motifs of autoinhibited kinases: discovery of ATP-independent inhibitors of fibroblast growth factor receptor. J Biol Chem. 2011 Jun 10;286(23):20677-87.

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