Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T66686 Target Info
Target Name Bacterial Penicillin-binding protein 1B (Bact mrcB)
Synonyms mrcB; PBP1b; PBP-1b; PBP 1b; Murein polymerase
Target Type Literature-reported Target
Gene Name Bact mrcB
Biochemical Class Acyltransferase
UniProt ID
PBPB_ECOLI
Drug Binding Sites of Target  Top
Ligand Name: (2R)-3-[[(2R,3R,4R,5S,6S)-3-[(2S,3R,4R,5S,6R)-3-acetamido-5-[(2S,3R,4R,5S,6R)-3-acetamido-4-hydroxy-6-methyl-5-[(2R,3R,4S,5R,6S)-3,4,5-trihydroxy-6-[(2-hydroxy-5-oxocyclopenta-1,3-dien-1-yl)carbamoyl]oxan-2-yl]oxyoxan-2-yl]oxy-4-hydroxy-6-[[(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxymethyl]oxan-2-yl]oxy-6-carbamoyl-4-carbamoyloxy-5-hydroxy-5-methyloxan-2-yl]oxy-hydroxyphosphoryl]oxy-2-(3,8,8,14,18-pentamethyl-11-methylidenenonadeca-2,6,13,17-tetraenoxy)propanoic acid Ligand Info
Structure Description Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli PDB:3VMA
Method X-ray diffraction Resolution 2.16 Å Mutation No [1]
PDB Sequence
LAIVFAVLIA
81
IYGVYLDQKI
91
RSRIDGKVWQ
101
LPAAVYGRMV
111
NLEPDMTISK
121

NEMVKLLEAT
131
QYRQVSKMTR
141
PGEFTVQANS
151
IEMIRRPFDF
161
PDSKEGQVRA
171

RLTFDGDHLA
181
TIVNMENNRQ
191
FGFFRLDPRL
201
ITMISSPNGE
211
QRLFVPRSGF
221

PDLLVDTLLA
231
TEDRHFYEHY
246
SIGRATLTQQ
271
LVKNLFLSSE
281
RSYWRKANEA
291

YMALIMDARY
301
SKDRILELYM
311
NEVYLGQSGD
321
NEIRGFPLAS
331
LYYFGRPVEE
341

LSLDQQALLV
351
GMVKGASIYN
361
PWRNPKLALE
371
RRNLVLRLLQ
381
QQQIIDQELY
391

DMLSARPLVQ
402
PRGGVISPQP
412
AFMQLVRQEL
422
QAKLGDKVKD
432
LSGVKIFTTF
442

DSVAQDAAEK
452
AAVEGIPALK
462
KQRKLSDLET
472
AIVVVDRFSG
482
EVRAMVGGSE
492

PQFAGYNRAM
502
QARRSIGSLA
512
KPATYLTALS
522
QPKIYRLNTW
532
IADAPIALRQ
542

PNGQVWSPQN
552
DDRRYSESGR
562
VMLVDALTRS
572
MNVPTVNLGM
582
ALGLPAVTET
592

WIKLGVPKDQ
602
LHPVPAMLLG
612
ALNLTPIEVA
622
QAFQTIASGG
632
NRAPLSALRS
642

VIAEDGKVLY
652
QSFPQAERAV
662
PAQAAYLTLW
672
TMQQVVQRGT
682
GRQLGAKYPN
692

LHLAGKTGTT
702
NNNVDTWFAG
712
IDGSTVTITW
722
VGRDNNQPTK
732
LYGASGAMSI
742

YQRYLANQTP
752
TPLNLVPPED
762
IADMGVDYDG
772
NFVCSGGMRI
782
LPVWTSDPQS
792

LCQQSEMQ
Residue
Distance (Å)
GLU233
2.576
GLN271
2.649
LYS274
2.756
ASN275
2.687
SER280
4.383
GLU281
2.591
ARG286
2.747
GLU290
4.541
TYR310
3.975
VAL314
4.129
Residue
Distance (Å)
TYR315
3.371
GLN318
3.669
GLU323
2.676
VAL354
3.011
LYS355
3.057
GLY356
3.792
ALA357
2.919
SER358
2.667
ILE359
3.495
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Selenomethionine Ligand Info
Structure Description Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli PDB:3FWL
Method X-ray diffraction Resolution 3.09 Å Mutation No [1]
PDB Sequence
LWLLLKLAIV
75
FAVLIAIYGV
85
YLDQKIRSRI
95
DGKVWQLPAA
105
VYGRVNLEPD
116

TISKNEVKLL
128
EATQYRQVSK
138
TRPGEFTVQA
149
NSIEIRRPFD
160
FPDSKEGQVR
170

ARLTFDGDHL
180
ATIVNENNRQ
191
FGFFRLDPRL
201
ITISSPNGEQ
212
RLFVPRSGFP
222

DLLVDTLLAT
232
EDRHFYEHDG
242
ISLYSILTQQ
271
LVKNLFLSSE
281
RSYWRKANEA
291

YALIDARYSK
303
DRILELYNEV
314
YLGQSGDNEI
324
RGFPLASLYY
334
FGRPVEELSL
344

DQQALLVGVK
355
GASIYNPWRN
365
PKLALERRNL
375
VLRLLQQQQI
385
IDQELYDLSA
396

RPVISPQPAF
414
QLVRQELQAK
425
LGDKVKDLSG
435
VKIFTTFDSV
445
AQDAAEKAAV
455

EGIPALKKQR
465
KLSDLETAIV
475
VVDRFSGEVR
485
AVGGSEPQFA
496
GYNRAQARRS
507

IGSLAKPATY
517
LTALSQPKIY
527
RLNTWIADAP
537
IALRQPNGQV
547
WSPQNDDRRY
557

SESGRVLVDA
568
LTRSNVPTVN
579
LGALGLPAVT
590
ETWIKLGVPK
600
DQLHPVPALL
611

GALNLTPIEV
621
AQAFQTIASG
631
GNRAPLSALR
641
SVIAEDGKVL
651
YQSFPQAERA
661

VPAQAAYLTL
671
WTQQVVQRGT
682
GRQLGAKYPN
692
LHLAGKTGTT
702
NNNVDTWFAG
712

IDGSTVTITW
722
VGRDNNQPTK
732
LYGASGASIY
743
QRYLANQTPT
753
PLNLVPPEDI
763

ADGVDYDGNF
774
VCSGGRILPV
785
WTSDPQSLCQ
795
QSE
Residue
Distance (Å)
LEU87
3.556
ILE91
3.494
ILE95
4.634
PRO103
3.414
ALA104
3.314
ALA105
4.256
VAL106
3.806
GLY108
3.774
ARG109
1.325
VAL111
1.328
ASN112
3.565
LEU113
3.835
GLU114
2.988
PRO115
3.087
ASP116
1.328
THR118
1.324
ILE119
3.075
SER120
2.799
LYS121
2.991
ASN122
3.195
GLU123
1.332
VAL125
1.328
LYS126
3.325
LEU127
3.011
LEU128
2.823
TYR133
3.278
VAL136
3.972
SER137
4.495
LYS138
1.332
THR140
1.330
ARG141
4.052
GLU144
3.449
PHE145
3.777
THR146
3.726
ILE152
3.674
GLU153
1.324
ILE155
1.324
ARG156
3.540
PHE159
3.180
ASP160
4.974
PHE161
3.392
PRO162
3.459
VAL169
3.419
ARG170
2.928
ALA171
2.829
ARG172
3.024
LEU173
3.595
PHE175
3.531
ASP178
4.769
HIS179
3.049
LEU180
2.951
VAL184
3.390
ASN185
1.325
GLU187
1.328
ASN188
3.747
ASN189
4.111
PHE195
4.030
ARG196
4.036
LEU197
3.551
ASP198
4.472
PRO199
3.125
LEU201
4.418
ILE202
3.346
THR203
1.329
ILE205
1.335
SER206
3.210
SER207
4.976
GLN212
2.985
ARG213
2.786
LEU214
3.868
PHE221
3.613
LEU225
3.565
VAL226
3.443
LEU229
3.469
GLN270
4.196
LEU272
4.614
VAL273
3.452
LYS274
4.650
PHE277
3.815
LEU278
3.415
ALA288
4.921
ASN289
2.925
GLU290
3.346
ALA291
3.155
TYR292
1.326
ALA294
1.330
LEU295
3.483
ILE296
1.327
ASP298
1.330
ALA299
2.866
ARG300
3.245
TYR301
3.062
ILE306
3.355
LEU307
3.041
GLU308
3.990
LEU309
3.363
TYR310
1.329
ASN312
1.328
GLU313
3.644
VAL314
4.978
TYR315
4.462
LEU316
3.497
GLY326
3.507
PHE327
2.917
PRO328
3.316
LEU329
4.406
TYR334
3.842
PHE335
4.868
ASP345
3.234
GLN346
3.364
LEU349
2.989
LEU350
3.457
VAL351
3.468
GLY352
1.331
VAL354
1.326
LYS355
2.817
GLY356
2.831
ALA357
3.077
TYR360
3.642
PRO362
3.233
LEU370
4.724
ARG372
4.528
ARG373
3.206
GLU389
4.778
TYR391
4.340
ASP392
1.331
LEU394
1.330
SER395
3.630
PRO410
4.542
GLN411
3.038
Residue
Distance (Å)
PRO412
3.942
ALA413
3.032
PHE414
1.328
GLN416
1.325
LEU417
3.166
VAL418
3.197
ARG419
2.662
GLN420
3.444
PHE439
3.328
GLN447
2.744
ILE474
3.462
VAL475
4.697
VAL484
4.604
ARG485
4.637
ALA486
1.328
VAL488
1.329
GLY489
4.051
ASN499
2.765
ARG500
3.127
ALA501
1.328
GLN503
1.332
ALA504
3.644
ALA512
4.029
LYS513
3.290
PRO514
4.788
TYR517
4.098
LEU529
4.043
ASN530
3.686
THR531
3.427
TRP532
3.347
ILE533
4.730
ASP535
3.746
LEU540
4.196
ASN552
4.003
SER558
4.605
ARG562
4.631
VAL563
1.328
LEU565
1.336
VAL566
3.114
ASP567
2.986
ALA568
2.630
LEU569
4.838
ARG571
3.441
SER572
1.329
ASN574
1.329
VAL575
3.903
PRO576
3.475
THR577
2.767
VAL578
2.773
ASN579
3.697
LEU580
2.976
GLY581
1.321
ALA583
1.324
LEU584
3.194
GLY585
3.451
LEU586
3.399
VAL589
3.832
THR590
3.580
TRP593
4.408
LEU603
4.725
HIS604
3.646
PRO605
4.078
VAL606
3.171
PRO607
2.880
ALA608
1.324
LEU610
1.328
LEU611
3.074
GLY612
2.811
ALA613
3.365
LEU614
4.815
THR617
3.471
PRO618
4.920
ILE619
4.138
PHE625
3.770
ILE628
4.821
LEU669
4.811
THR670
2.728
LEU671
2.641
TRP672
3.349
THR673
1.327
GLN675
1.323
GLN676
2.964
VAL677
2.739
VAL678
3.027
THR682
4.216
GLY683
2.987
ARG684
4.020
GLN685
3.242
LEU686
3.290
LEU695
4.462
ALA696
3.878
GLY697
3.334
LYS698
3.403
THR699
4.138
PHE710
3.564
ALA711
4.742
ILE713
4.835
ALA736
3.016
SER737
3.766
GLY738
3.054
ALA739
1.325
SER741
1.327
ILE742
3.384
TYR743
3.700
GLN744
2.966
ALA764
3.228
ASP765
1.329
GLY767
1.321
VAL768
3.249
ASP769
3.604
TYR770
3.953
ASP771
4.338
GLY772
3.064
PHE774
3.977
GLY778
4.543
GLY779
1.326
ARG781
1.321
ILE782
3.241
LEU783
2.804
PRO784
4.965
VAL785
3.576
THR787
4.558
PRO790
3.725
SER792
4.485
LEU793
3.414
GLN795
3.698
GLN796
3.738
SER797
4.318
GLU798
1.330
Ligand Name: (2S)-5-methylidene-2-[(1R)-2-oxo-1-[(2-thiophen-2-ylacetyl)amino]ethyl]-2H-1,3-thiazine-4-carboxylic acid Ligand Info
Structure Description E. coli PBP1b in complex with acyl-CENTA and moenomycin PDB:5HLD
Method X-ray diffraction Resolution 2.31 Å Mutation No [2]
PDB Sequence
AIVFAVLIAI
82
YGVYLDQKIR
92
SRIDGKVWQL
102
PAAVYGRMVN
112
LEPDMTISKN
122

EMVKLLEATQ
132
YRQVSKMTRP
142
GEFTVQANSI
152
EMIRRPFDFP
162
DSKEGQVRAR
172

LTFDGDHLAT
182
IVNMENNRQF
192
GFFRLDPRLI
202
TMISSPNGEQ
212
RLFVPRSGFP
222

DLLVDTLLAT
232
ETQQLVKNLF
277
LSKANEAYMA
294
LIMDARYSKD
304
RILELYMNEV
314

YLGQSGDNEI
324
RGFPLASLYY
334
FGRPVEELSL
344
DQQALLVGMV
354
LALERRNLVL
377

RLLYDMLSAR
397
PQPAFMQLVR
419
QELQAKLGDK
429
VKDLSGVKIF
439
TTFDSVAQDA
449

AEKAAVEGIP
459
ALKKQRKLSD
469
LETAIVVVDR
479
FSGEVRAMVG
489
GSEPQFAGYN
499

RAMQARRSIG
509
SLAKPATYLT
519
ALSQPKIYRL
529
NTWIADAPIA
539
LRQPNGQVWS
549

PQNDDRRYSE
559
SGRVMLVDAL
569
TRSMNVPTVN
579
LGMALGLPAV
589
TETWIKLGVP
599

KDQLHPVPAM
609
LLGALNLTPI
619
EVAQAFQTIA
629
SGGNRAPLSA
639
LRSVIAEDGK
649

VLYQSFPQAE
659
RAVPAQAAYL
669
TLWTMQQVVQ
679
RGTGRQLGAK
689
YPNLHLAGKT
699

GTTNNNVDTW
709
FAGIDGSTVT
719
ITWVGRDNNQ
729
PTKLYGASGA
739
MSIYQRYLAN
749

QTPTPLNLVP
759
PEDIADMGVD
769
YDGNFVCSGG
779
MRILPVWTSD
789
PQSLCQQSE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .63V or .63V2 or .63V3 or :363V;style chemicals stick;color identity;select .A:509 or .A:510 or .A:513 or .A:551 or .A:553 or .A:572 or .A:574 or .A:611 or .A:682 or .A:698 or .A:699 or .A:700 or .A:701 or .A:702 or .A:703 or .A:704 or .A:705 or .A:734 or .A:735 or .A:736; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY509
4.000
SER510
1.447
LYS513
3.746
GLN551
4.602
ASP553
3.468
SER572
3.658
ASN574
2.544
LEU611
4.782
THR682
3.499
LYS698
4.042
Residue
Distance (Å)
THR699
2.458
GLY700
3.876
THR701
2.583
THR702
3.260
ASN703
3.620
ASN704
4.683
ASN705
4.220
TYR734
3.928
GLY735
3.945
ALA736
4.950
Ligand Name: (2S)-2-[(1R)-1-[[(2R)-2-amino-2-phenylacetyl]amino]-2-oxoethyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid Ligand Info
Structure Description E. coli PBP1b in complex with acyl-cephalexin and moenomycin PDB:5HLA
Method X-ray diffraction Resolution 2.36 Å Mutation No [2]
PDB Sequence
WLLLKLAIVF
76
AVLIAIYGVY
86
LDQKIRSRID
96
GKVWQLPAAV
106
YGRMVNLEPD
116

MTISKNEMVK
126
LLEATQYRQV
136
SKMTRPGEFT
146
VQANSIEMIR
156
RPFDFPDSKE
166

GQVRARLTFD
176
GDHLATIVNM
186
ENNRQFGFFR
196
LDPRLITMIS
206
SPNGEQRLFV
216

PRSGFPDLLV
226
DTLLATEDRH
236
FYETLTQQLV
273
KNLFLSKANE
290
AYMALIMDAR
300

YSKDRILELY
310
MNEVYLGQSG
320
DNEIRGFPLA
330
SLYYFGRPVE
340
ELSLDQQALL
350

VGMVKGASIY
360
NPWRNPKLAL
370
ERRNLVLRLL
380
QQQQIIDQEL
390
YDMLSARPLQ
402

PRGGVISPQP
412
AFMQLVRQEL
422
QAKLGDKVKD
432
LSGVKIFTTF
442
DSVAQDAAEK
452

AAVEGIPALK
462
KQRKLSDLET
472
AIVVVDRFSG
482
EVRAMVGGSE
492
PQFAGYNRAM
502

QARRSIGSLA
512
KPATYLTALS
522
QPKIYRLNTW
532
IADAPIALRQ
542
PNGQVWSPQN
552

DDRRYSESGR
562
VMLVDALTRS
572
MNVPTVNLGM
582
ALGLPAVTET
592
WIKLGVPKDQ
602

LHPVPAMLLG
612
ALNLTPIEVA
622
QAFQTIASGG
632
NRAPLSALRS
642
VIAEDGKVLY
652

QSFPQAERAV
662
PAQAAYLTLW
672
TMQQVVQRGT
682
GRQLGAKYPN
692
LHLAGKTGTT
702

NNNVDTWFAG
712
IDGSTVTITW
722
VGRDNNQPTK
732
LYGASGAMSI
742
YQRYLANQTP
752

TPLNLVPPED
762
IADMGVDYDG
772
NFVCSGGMRI
782
LPVWTSDPQS
792
LCQQSEM
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .63U or .63U2 or .63U3 or :363U;style chemicals stick;color identity;select .A:509 or .A:510 or .A:513 or .A:553 or .A:572 or .A:574 or .A:611 or .A:682 or .A:698 or .A:699 or .A:700 or .A:701 or .A:702 or .A:703 or .A:705 or .A:734 or .A:735 or .A:736; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY509
3.710
SER510
1.274
LYS513
3.676
ASP553
3.437
SER572
3.213
ASN574
2.689
LEU611
4.844
THR682
3.319
LYS698
4.326
Residue
Distance (Å)
THR699
2.613
GLY700
3.528
THR701
2.729
THR702
3.710
ASN703
3.361
ASN705
4.203
TYR734
4.142
GLY735
3.849
ALA736
4.801
Ligand Name: 2-[(Z)-[1-(2-amino-1,3-thiazol-4-yl)-2-oxo-2-[[(2S,3S)-1-oxo-3-(sulfoamino)butan-2-yl]amino]ethylidene]amino]oxy-2-methylpropanoic acid Ligand Info
Structure Description E. coli PBP1b in complex with acyl-aztreonam and moenomycin PDB:5HLB
Method X-ray diffraction Resolution 2.42 Å Mutation No [2]
PDB Sequence
WLLLKLAIVF
76
AVLIAIYGVY
86
LDQKIRSRID
96
GKVWQLPAAV
106
YGRMVNLEPD
116

MTISKNEMVK
126
LLEATQYRQV
136
SKMTRPGEFT
146
VQANSIEMIR
156
RPFDFPDSKE
166

GQVRARLTFD
176
GDHLATIVNM
186
ENNRQFGFFR
196
LDPRLITMIS
206
SPNGEQRLFV
216

PRSGFPDLLV
226
DTLLATEDRH
236
FYEHDGISLY
246
SIGRAVLANL
256
TAGRTVQGAS
266

TLTQQLVKNL
276
FLSSERSYWR
286
KANEAYMALI
296
MDARYSKDRI
306
LELYMNEVYL
316

GQSGDNEIRG
326
FPLASLYYFG
336
RPVEELSLDQ
346
QALLVGMVKG
356
ASIYNPWRNP
366

KLALERRNLV
376
LRLLQQQQII
386
DQELYDMLSA
396
RPLGVQPRGG
406
VISPQPAFMQ
416

LVRQELQAKL
426
GDKVKDLSGV
436
KIFTTFDSVA
446
QDAAEKAAVE
456
GIPALKKQRK
466

LSDLETAIVV
476
VDRFSGEVRA
486
MVGGSEPQFA
496
GYNRAMQARR
506
SIGSLAKPAT
516

YLTALSQPKI
526
YRLNTWIADA
536
PIALRQPNGQ
546
VWSPQNDDRR
556
YSESGRVMLV
566

DALTRSMNVP
576
TVNLGMALGL
586
PAVTETWIKL
596
GVPKDQLHPV
606
PAMLLGALNL
616

TPIEVAQAFQ
626
TIASGGNRAP
636
LSALRSVIAE
646
DGKVLYQSFP
656
QAERAVPAQA
666

AYLTLWTMQQ
676
VVQRGTGRQL
686
GAKYPNLHLA
696
GKTGTTNNNV
706
DTWFAGIDGS
716

TVTITWVGRD
726
NNQPTKLYGA
736
SGAMSIYQRY
746
LANQTPTPLN
756
LVPPEDIADM
766

GVDYDGNFVC
776
SGGMRILPVW
786
TSDPQSLCQQ
796
SEM
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .AZR or .AZR2 or .AZR3 or :3AZR;style chemicals stick;color identity;select .A:507 or .A:509 or .A:510 or .A:513 or .A:551 or .A:553 or .A:572 or .A:574 or .A:611 or .A:612 or .A:613 or .A:682 or .A:698 or .A:699 or .A:700 or .A:701 or .A:702 or .A:703 or .A:704 or .A:734 or .A:735 or .A:736; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER507
3.399
GLY509
3.965
SER510
1.461
LYS513
4.082
GLN551
4.901
ASP553
3.619
SER572
3.760
ASN574
3.562
LEU611
2.944
GLY612
3.975
ALA613
4.670
Residue
Distance (Å)
THR682
3.307
LYS698
4.507
THR699
2.763
GLY700
3.332
THR701
2.804
THR702
3.277
ASN703
2.720
ASN704
4.429
TYR734
3.749
GLY735
3.985
ALA736
4.603
Ligand Name: (2r,4s)-2-[(1r)-1-{[(2r)-2-Amino-2-Phenylacetyl]amino}-2-Oxoethyl]-5,5-Dimethyl-1,3-Thiazolidine-4-Carboxylic Acid Ligand Info
Structure Description E. coli PBP1b in complex with acyl-ampicillin and moenomycin PDB:5HL9
Method X-ray diffraction Resolution 2.70 Å Mutation No [2]
PDB Sequence
LLLKLAIVFA
77
VLIAIYGVYL
87
DQKIRSRIDG
97
KVWQLPAAVY
107
GRMVNLEPDM
117

TISKNEMVKL
127
LEATQYRQVS
137
KMTRPGEFTV
147
QANSIEMIRR
157
PFDFPDSKEG
167

QVRARLTFDG
177
DHLATIVNME
187
NNRQFGFFRL
197
DPRLITMISN
209
GEQRLFVPRS
219

GFPDLLVDTL
229
LATEDRHFYT
267
LTQQLVKNLF
277
LSSERSYWRK
287
ANEAYMALIM
297

DARYSKDRIL
307
ELYMNEVYLG
317
QSGDNEIRGF
327
PLASLYYFGR
337
PVEELSLDQQ
347

ALLVGMVKGA
357
SIYNPWRNPK
367
LALERRNLVL
377
RLLQQQQIID
387
QELYDMLSAR
397

PLGVQPRGIS
409
PQPAFMQLVR
419
QELQAKLVKD
432
LSGVKIFTTF
442
DSVAQDAAEK
452

AAVEGIPALK
462
KQRKLSDLET
472
AIVVVDRFSG
482
EVRAMVGGSE
492
PQFAGYNRAM
502

QARRSIGSLA
512
KPATYLTALS
522
QPKIYRLNTW
532
IADAPIALRQ
542
PNGQVWSPQN
552

DDRRYSESGR
562
VMLVDALTRS
572
MNVPTVNLGM
582
ALGLPAVTET
592
WIKLGVPKDQ
602

LHPVPAMLLG
612
ALNLTPIEVA
622
QAFQTIASGG
632
NRAPLSALRS
642
VIAEDGKVLY
652

QSFPQAERAV
662
PAQAAYLTLW
672
TMQQVVQRGT
682
GRQLGAKYPN
692
LHLAGKTGTT
702

NNNVDTWFAG
712
IDGSTVTITW
722
VGRDNNQPTK
732
LYGASGAMSI
742
YQRYLANQTP
752

TPLNLVPPED
762
IADMGVDYDG
772
NFVCSGGMRI
782
LPVWTSDPQS
792
LCQQS
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .AIX or .AIX2 or .AIX3 or :3AIX;style chemicals stick;color identity;select .A:509 or .A:510 or .A:513 or .A:552 or .A:553 or .A:554 or .A:571 or .A:572 or .A:574 or .A:611 or .A:682 or .A:698 or .A:699 or .A:700 or .A:701 or .A:702 or .A:703 or .A:704 or .A:705 or .A:734 or .A:735; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY509
3.980
SER510
1.421
LYS513
3.003
ASN552
4.809
ASP553
2.944
ASP554
4.785
ARG571
3.974
SER572
2.256
ASN574
2.957
LEU611
4.769
THR682
3.235
Residue
Distance (Å)
LYS698
3.621
THR699
2.969
GLY700
3.424
THR701
2.256
THR702
3.026
ASN703
2.166
ASN704
4.822
ASN705
3.535
TYR734
2.767
GLY735
3.832
Ligand Name: [[(3R,6S)-1-formyl-6-[[(3S)-pyrrolidin-3-yl]oxycarbamoyl]piperidin-3-yl]amino] hydrogen sulfate Ligand Info
Structure Description E. coli PBP1b in complex with FPI-1465 PDB:5FGZ
Method X-ray diffraction Resolution 2.85 Å Mutation No [3]
PDB Sequence
LAIVFAVLIA
81
IYGVYLDQKI
91
RSRIDGKVWQ
101
LPAAVYGRMV
111
NLEPDMTISK
121

NEMVKLLEAT
131
QYRQVSKMTR
141
PGEFTVQANS
151
IEMIRRPFDF
161
PDSKEGQVRA
171

RLTFDGDHLA
181
TIVNMENNRQ
191
FGFFRLDPRL
201
ITMISSPNGE
211
QRLFVPRSGF
221

PDLLVDTLLA
231
TEDTLTQQLV
273
KNLFLSSERS
283
YWRKANEAYM
293
ALIMDARYSK
303

DRILELYMNE
313
VYLGQSGDNE
323
IRGFPLASLY
333
YFGRPVEELS
343
LDQQALLVGM
353

VKGASIYNPW
363
RNPKLALERR
373
NLVLRLLQQQ
383
QIIDQELYDM
393
LSARPLGVQP
403

RGGVISPQPA
413
FMQLVRQELQ
423
AKLGDKVKDL
433
SGVKIFTTFD
443
SVAQDAAEKA
453

AVEGIPALKK
463
QRKLSDLETA
473
IVVVDRFSGE
483
VRAMVGGSEP
493
QFAGYNRAMQ
503

ARRSIGSLAK
513
PATYLTALSQ
523
PKIYRLNTWI
533
ADAPIALRQP
543
NGQVWSPQND
553

DRRYSESGRV
563
MLVDALTRSM
573
NVPTVNLGMA
583
LGLPAVTETW
593
IKLGVPKDQL
603

HPVPAMLLGA
613
LNLTPIEVAQ
623
AFQTIASGGN
633
RAPLSALRSV
643
IAEDGKVLYQ
653

SFPQAERAVP
663
AQAAYLTLWT
673
MQQVVQRGTG
683
RQLGAKYPNL
693
HLAGKTGTTN
703

NNVDTWFAGI
713
DGSTVTITWV
723
GRDNNQPTKL
733
YGASGAMSIY
743
QRYLANQTPT
753

PLNLVPPEDI
763
ADMGVDYDGN
773
FVCSGGMRIL
783
PVWTSDPQSL
793
CQQSEMQ
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .5VW or .5VW2 or .5VW3 or :35VW;style chemicals stick;color identity;select .A:507 or .A:509 or .A:510 or .A:513 or .A:553 or .A:571 or .A:572 or .A:574 or .A:611 or .A:612 or .A:613 or .A:682 or .A:698 or .A:699 or .A:700 or .A:701 or .A:702 or .A:703 or .A:735 or .A:736; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER507
3.709
GLY509
3.048
SER510
1.415
LYS513
2.625
ASP553
2.913
ARG571
4.331
SER572
2.388
ASN574
2.659
LEU611
3.068
GLY612
3.075
Residue
Distance (Å)
ALA613
3.885
THR682
2.802
LYS698
4.238
THR699
3.169
GLY700
3.367
THR701
2.273
THR702
2.314
ASN703
1.982
GLY735
4.599
ALA736
3.927
References  Top
REF 1 Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli. Proc Natl Acad Sci U S A. 2009 Jun 2;106(22):8824-9.
REF 2 Structural Insights into Inhibition of Escherichia coli Penicillin-binding Protein 1B. J Biol Chem. 2017 Jan 20;292(3):979-993.
REF 3 Structural and Kinetic Characterization of Diazabicyclooctanes as Dual Inhibitors of Both Serine-Beta-Lactamases and Penicillin-Binding Proteins. ACS Chem Biol. 2016 Apr 15;11(4):864-8.

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