Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T65889 Target Info
Target Name Pyruvate kinase M2 (PKM)
Synonyms p58; Tumor M2-PK; Thyroid hormone-binding protein 1; THBP1; Pyruvate kinase muscle isozyme; Pyruvate kinase isozymes M1/M2; Pyruvate kinase PKM; Pyruvate kinase 2/3; PKM2; PK3; PK2; Opa-interacting protein 3; OIP3; OIP-3; Cytosolic thyroid hormone-binding protein; CTHBP
Target Type Clinical trial Target
Gene Name PKM
Biochemical Class Kinase
UniProt ID
KPYM_HUMAN
Ligand General Information  Top
Ligand Name 1,6-di-O-phosphono-beta-D-fructofuranose Ligand Info
Canonical SMILES C(C1C(C(C(O1)(COP(=O)(O)O)O)O)O)OP(=O)(O)O
InChI 1S/C6H14O12P2/c7-4-3(1-16-19(10,11)12)18-6(9,5(4)8)2-17-20(13,14)15/h3-5,7-9H,1-2H2,(H2,10,11,12)(H2,13,14,15)/t3-,4-,5+,6-/m1/s1
InChIKey RNBGYGVWRKECFJ-ARQDHWQXSA-N
PubChem Compound ID 10267
Drug Binding Sites of Target  Top
PDB ID: 3U2Z      Activator-Bound Structure of Human Pyruvate Kinase M2
Method X-ray diffraction Resolution 2.10 Å Mutation No [1]
PDB Sequence
IQTQQLHAAM
22
ADTFLEHMCR
32
LDIDSPPITA
42
RNTGIICTIG
52
PASRSVETLK
62

EMIKSGMNVA
72
RLNFSHGTHE
82
YHAETIKNVR
92
TATESFASDP
102
ILYRPVAVAL
112

DTKGPEIRTG
122
LIKGSGTAEV
132
ELKKGATLKI
142
TLDNAYMEKC
152
DENILWLDYK
162

NICKVVEVGS
172
KIYVDDGLIS
182
LQVKQKGADF
192
LVTEVENGGS
202
LGSKKGVNLP
212

GAAVDLPAVS
222
EKDIQDLKFG
232
VEQDVDMVFA
242
SFIRKASDVH
252
EVRKVLGEKG
262

KNIKIISKIE
272
NHEGVRRFDE
282
ILEASDGIMV
292
ARGDLGIEIP
302
AEKVFLAQKM
312

MIGRCNRAGK
322
PVICATQMLE
332
SMIKKPRPTR
342
AEGSDVANAV
352
LDGADCIMLS
362

GETAKGDYPL
372
EAVRMQHLIA
382
REAEAAIYHL
392
QLFEELRRLA
402
PITSDPTEAT
412

AVGAVEASFK
422
CCSGAIIVLT
432
KSGRSAHQVA
442
RYRPRAPIIA
452
VTRNPQTARQ
462

AHLYRGIFPV
472
LCKDPVQEAW
482
AEDVDLRVNF
492
AMNVGKARGF
502
FKKGDVVIVL
512

TGWRPGSGFT
522
NTMRVVPVP
Residue
Distance (Å)
LEU431
3.505
THR432
2.539
LYS433
3.156
SER434
2.614
GLY435
4.082
ARG436
3.713
SER437
2.700
ALA438
4.866
TRP482
2.810
ASP485
4.694
VAL486
4.876
Residue
Distance (Å)
ARG489
2.737
THR513
3.988
GLY514
3.060
TRP515
3.988
ARG516
2.782
PRO517
3.613
GLY518
2.505
SER519
2.505
GLY520
2.906
PHE521
3.033
THR522
3.483
PDB ID: 4RPP      crystal structure of PKM2-K422R mutant bound with FBP
Method X-ray diffraction Resolution 2.58 Å Mutation Yes [2]
PDB Sequence
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63
MIKSGMNVAR
73

LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113
TKGPEINLPG
213

AAVDLPAVSE
223
KDIQDLKFGV
233
EQDVDMVFAS
243
FIRKASDVHE
253
VRKVLGEKGK
263

NIKIISKIEN
273
HEGVRRFDEI
283
LEASDGIMVA
293
RGDLGIEIPA
303
EKVFLAQKMM
313

IGRCNRAGKP
323
VICATQMLES
333
MIKKPRPTRA
343
EGSDVANAVL
353
DGADCIMLSG
363

ETAKGDYPLE
373
AVRMQHLIAR
383
EAEAAIYHLQ
393
LFEELRRLAP
403
ITSDPTEATA
413

VGAVEASFRC
423
CSGAIIVLTK
433
SGRSAHQVAR
443
YRPRAPIIAV
453
TRNPQTARQA
463

HLYRGIFPVL
473
CKDPVQEAWA
483
EDVDLRVNFA
493
MNVGKARGFF
503
KKGDVVIVLT
513

GTNTMRVVPV
530
P
Residue
Distance (Å)
LEU431
3.423
THR432
2.700
LYS433
2.307
SER434
2.550
GLY435
4.305
ARG436
3.947
SER437
2.706
Residue
Distance (Å)
TRP482
3.262
ASP485
4.754
ARG489
2.466
LEU512
4.967
THR513
4.020
GLY514
2.990
THR522
3.948
PDB ID: 3BJF      Pyruvate kinase M2 is a phosphotyrosine binding protein
Method X-ray diffraction Resolution 2.03 Å Mutation No [3]
PDB Sequence
QTQQLHAAMA
23
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63

MIKSGMNVAR
73
LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113

TKGPEIRTGL
123
IKGSGTAEVE
133
LKKGATLKIT
143
LDNAYMEKCD
153
ENILWLDYKN
163

ICKVVEVGSK
173
IYVDDGLISL
183
QVKQKGADFL
193
VTEVENGGSL
203
GSKKGVNLPG
213

AAVDLPAVSE
223
KDIQDLKFGV
233
EQDVDMVFAS
243
FIRKASDVHE
253
VRKVLGEKGK
263

NIKIISKIEN
273
HEGVRRFDEI
283
LEASDGIMVA
293
RGDLGIEIPA
303
EKVFLAQKMM
313

IGRCNRAGKP
323
VICATQMLES
333
MIKKPRPTRA
343
EGSDVANAVL
353
DGADCIMLSG
363

ETAKGDYPLE
373
AVRMQNLIAR
383
EAEAAIYHLQ
393
LFEELRRLAP
403
ITSDPTEATA
413

VGAVEASFKC
423
CSGAIIVLTK
433
SGRSAHQVAR
443
YRPRAPIIAV
453
TRNPQTARQA
463

HLYRGIFPVL
473
CKDPVQEAWA
483
EDVDLRVNFA
493
MNVGKARGFF
503
KKGDVVIVLT
513

GWRPGSGFTN
523
TMRVVPVP
Residue
Distance (Å)
LEU431
3.612
THR432
2.664
LYS433
3.164
SER434
2.537
GLY435
3.960
ARG436
3.780
SER437
2.627
ALA438
4.982
TRP482
3.205
ASP485
4.504
ARG489
3.337
Residue
Distance (Å)
THR513
4.543
GLY514
3.012
TRP515
3.989
ARG516
2.852
PRO517
3.447
GLY518
2.782
SER519
2.671
GLY520
2.790
PHE521
2.739
THR522
3.170
PDB ID: 4B2D      human PKM2 with L-serine and FBP bound.
Method X-ray diffraction Resolution 2.30 Å Mutation No [4]
PDB Sequence
> Chain A
QTQQLHAAMA
23
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63

MIKSGMNVAR
73
LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113

TKGPEIRTGL
123
IKGSGTAEVE
133
LKKGATLKIT
143
LDNAYMEKCD
153
ENILWLDYKN
163

ICKVVEVGSK
173
IYVDDGLISL
183
QVKQKGADFL
193
VTEVENGGSL
203
GSKKGVNLPG
213

AAVDLPAVSE
223
KDIQDLKFGV
233
EQDVDMVFAS
243
FIRKASDVHE
253
VRKVLGEKGK
263

NIKIISKIEN
273
HEGVRRFDEI
283
LEASDGIMVA
293
RGDLGIEIPA
303
EKVFLAQKMM
313

IGRCNRAGKP
323
VICATQMLES
333
MIKKPRPTRA
343
EGSDVANAVL
353
DGADCIMLSG
363

ETAKGDYPLE
373
AVRMQHLIAR
383
EAEAAIYHLQ
393
LFEELRRLAP
403
ITSDPTEATA
413

VGAVEASFKC
423
CSGAIIVLTK
433
SGRSAHQVAR
443
YRPRAPIIAV
453
TRNPQTARQA
463

HLYRGIFPVL
473
CKDPVQEAWA
483
EDVDLRVNFA
493
MNVGKARGFF
503
KKGDVVIVLT
513

GWRPGSGFTN
523
TMRVVPVP
> Chain D
QTQQLHAAMA
23
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63

MIKSGMNVAR
73
LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113

TKGPEIRTGL
123
IKGSGTAEVE
133
LKKGATLKLT
143
LDNAYMEKCD
153
ENILWLDYKN
163

ICKVVEVGSK
173
IYVDDGLISL
183
QVKQKGADFL
193
VTEVENGGSL
203
GSKKGVNLPG
213

AAVDLPAVSE
223
KDIQDLKFGV
233
EQDVDMVFAS
243
FIRKASDVHE
253
VRKVLGEKGK
263

NIKIISKIEN
273
HEGVRRFDEI
283
LEASDGIMVA
293
RGDLGIEIPA
303
EKVFLAQKMM
313

IGRCNRAGKP
323
VICATQMLES
333
MIKKPRPTRA
343
EGSDVANAVL
353
DGADCIMLSG
363

ETAKGDYPLE
373
AVRMQHLIAR
383
EAEAAIYHLQ
393
LFEELRRLAP
403
ITSDPTEATA
413

VGAVEASFKC
423
CSGAIIVLTK
433
SGRSAHQVAR
443
YRPRAPIIAV
453
TRNPQTARQA
463

HLYRGIFPVL
473
CKDPVQEAWA
483
EDVDLRVNFA
493
MNVGKARGFF
503
KKGDVVIVLT
513

GWRPGSGFTN
523
TMRVVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:485 or .A:486 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522 or .D:431 or .D:432 or .D:433 or .D:434 or .D:435 or .D:436 or .D:437 or .D:438 or .D:482 or .D:485 or .D:486 or .D:489 or .D:513 or .D:514 or .D:515 or .D:516 or .D:517 or .D:518 or .D:519 or .D:520 or .D:521 or .D:522; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue [Chain]
Distance (Å)
LEU431[A]
3.652
THR432[A]
2.653
LYS433[A]
3.062
SER434[A]
2.630
GLY435[A]
4.176
ARG436[A]
3.798
SER437[A]
2.736
ALA438[A]
4.866
TRP482[A]
2.739
ASP485[A]
4.634
VAL486[A]
4.821
ARG489[A]
2.739
THR513[A]
4.100
GLY514[A]
3.145
TRP515[A]
4.086
ARG516[A]
2.632
PRO517[A]
3.402
GLY518[A]
2.571
SER519[A]
2.597
GLY520[A]
2.681
PHE521[A]
2.872
THR522[A]
3.386
Residue [Chain]
Distance (Å)
LEU431[D]
3.749
THR432[D]
2.610
LYS433[D]
3.040
SER434[D]
2.604
GLY435[D]
4.087
ARG436[D]
3.722
SER437[D]
2.643
ALA438[D]
4.842
TRP482[D]
2.718
ASP485[D]
4.800
VAL486[D]
4.724
ARG489[D]
2.746
THR513[D]
4.103
GLY514[D]
3.085
TRP515[D]
4.040
ARG516[D]
2.679
PRO517[D]
3.389
GLY518[D]
2.581
SER519[D]
2.715
GLY520[D]
2.813
PHE521[D]
2.866
THR522[D]
3.310
PDB ID: 6TTI      PKM2 in complex with Compound 6
Method Electron microscopy Resolution 2.50 Å Mutation No [5]
PDB Sequence
HAAMADTFLE
28
HMCRLDIDSP
38
PITARNTGII
48
CTIGPASRSV
58
ETLKEMIKSG
68

MNVARLNFSH
78
GTHEYHAETI
88
KNVRTATESF
98
ASDPILYRPV
108
AVALDTKGPE
118

IRLPAVSEKD
225
IQDLKFGVEQ
235
DVDMVFASFI
245
RKASDVHEVR
255
KVLGEKGKNI
265

KIISKIENHE
275
GVRRFDEILE
285
ASDGIMVARG
295
DLGIEIPAEK
305
VFLAQKMMIG
315

RCNRAGKPVI
325
CATQMLESMI
335
KKPRPTRAEG
345
SDVANAVLDG
355
ADCIMLSGET
365

AKGDYPLEAV
375
RMQHLIAREA
385
EAAIYHLQLF
395
EELRRLAPIT
405
SDPTEATAVG
415

AVEASFKCCS
425
GAIIVLTKSG
435
RSAHQVARYR
445
PRAPIIAVTR
455
NPQTARQAHL
465

YRGIFPVLCK
475
DPVQEAWAED
485
VDLRVNFAMN
495
VGKARGFFKK
505
GDVVIVLTGW
515

RPGSGFTNTM
525
RVVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:482 or .A:485 or .A:486 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.628
THR432
2.627
LYS433
3.202
SER434
2.780
GLY435
4.081
ARG436
3.760
SER437
3.016
TRP482
2.997
ASP485
4.688
VAL486
4.923
ARG489
2.813
Residue
Distance (Å)
THR513
4.298
GLY514
3.216
TRP515
4.094
ARG516
2.711
PRO517
3.751
GLY518
2.764
SER519
2.792
GLY520
3.361
PHE521
2.884
THR522
3.596
PDB ID: 6TTH      PKM2 in complex with L-threonine
Method Electron microscopy Resolution 2.60 Å Mutation No [5]
PDB Sequence
MADTFLEHMC
31
RLDIDSPPIT
41
ARNTGIICTI
51
GPASRSVETL
61
KEMIKSGMNV
71

ARLNFSHGTH
81
EYHAETIKNV
91
RTATESFASD
101
PILYRPVAVA
111
LDTKGPLPAV
221

SEKDIQDLKF
231
GVEQDVDMVF
241
ASFIRKASDV
251
HEVRKVLGEK
261
GKNIKIISKI
271

ENHEGVRRFD
281
EILEASDGIM
291
VARGDLGIEI
301
PAEKVFLAQK
311
MMIGRCNRAG
321

KPVICATQML
331
ESMIKKPRPT
341
RAEGSDVANA
351
VLDGADCIML
361
SGETAKGDYP
371

LEAVRMQHLI
381
AREAEAAIYH
391
LQLFEELRRL
401
APITSDPTEA
411
TAVGAVEASF
421

KCCSGAIIVL
431
TKSGRSAHQV
441
ARYRPRAPII
451
AVTRNPQTAR
461
QAHLYRGIFP
471

VLCKDPVQEA
481
WAEDVDLRVN
491
FAMNVGKARG
501
FFKKGDVVIV
511
LTGWRPGSGF
521

TNTMRVVPVP
531
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:485 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.613
THR432
2.732
LYS433
3.291
SER434
2.806
GLY435
4.135
ARG436
3.489
SER437
2.708
ALA438
4.884
TRP482
3.143
ASP485
4.598
ARG489
2.733
Residue
Distance (Å)
THR513
4.106
GLY514
3.095
TRP515
3.988
ARG516
2.624
PRO517
3.588
GLY518
2.488
SER519
2.638
GLY520
2.792
PHE521
2.875
THR522
3.433
PDB ID: 6TTQ      PKM2 in complex with Compound 10
Method Electron microscopy Resolution 2.70 Å Mutation No [5]
PDB Sequence
MADTFLEHMC
31
RLDIDSPPIT
41
ARNTGIICTI
51
GPASRSVETL
61
KEMIKSGMNV
71

ARLNFSHGTH
81
EYHAETIKNV
91
RTATESFASD
101
PILYRPVAVA
111
LDTKGPEIRT
121

GLIKGSGTAE
131
VELKKGATLK
141
ITLDNAYMEK
151
CDENILWLDY
161
KNICKVVEVG
171

SKIYVDDGLI
181
SLQVKQKGAD
191
FLVTEVENGG
201
SLGSKKGVNL
211
PGAAVDLPAV
221

SEKDIQDLKF
231
GVEQDVDMVF
241
ASFIRKASDV
251
HEVRKVLGEK
261
GKNIKIISKI
271

ENHEGVRRFD
281
EILEASDGIM
291
VARGDLGIEI
301
PAEKVFLAQK
311
MMIGRCNRAG
321

KPVICATQML
331
ESMIKKPRPT
341
RAEGSDVANA
351
VLDGADCIML
361
SGETAKGDYP
371

LEAVRMQHLI
381
AREAEAAIYH
391
LQLFEELRRL
401
APITSDPTEA
411
TAVGAVEASF
421

KCCSGAIIVL
431
TKSGRSAHQV
441
ARYRPRAPII
451
AVTRNPQTAR
461
QAHLYRGIFP
471

VLCKDPVQEA
481
WAEDVDLRVN
491
FAMNVGKARG
501
FFKKGDVVIV
511
LTGWRPGSGF
521

TNTMRVVPVP
531
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:482 or .A:485 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.788
THR432
2.650
LYS433
3.506
SER434
2.707
GLY435
4.185
ARG436
3.774
SER437
2.307
TRP482
3.199
ASP485
4.975
ARG489
2.804
Residue
Distance (Å)
THR513
4.269
GLY514
3.398
TRP515
4.177
ARG516
2.544
PRO517
3.625
GLY518
3.021
SER519
2.751
GLY520
3.082
PHE521
2.869
THR522
3.831
PDB ID: 6TTF      PKM2 in complex with Compound 5
Method Electron microscopy Resolution 3.20 Å Mutation No [5]
PDB Sequence
LHAAMADTFL
27
EHMCRLDIDS
37
PPITARNTGI
47
ICTIGPASRS
57
VETLKEMIKS
67

GMNVARLNFS
77
HGTHEYHAET
87
IKNVRTATES
97
FASDPILYRP
107
VAVALDTKGP
117

EIRTGLIKGS
127
GTAEVELKKG
137
ATLKITLDNA
147
YMEKCDENIL
157
WLDYKNICKV
167

VEVGSKIYVD
177
DGLISLQVKQ
187
KGADFLVTEV
197
ENGGSLGSKK
207
GVNLPGAAVD
217

LPAVSEKDIQ
227
DLKFGVEQDV
237
DMVFASFIRK
247
ASDVHEVRKV
257
LGEKGKNIKI
267

ISKIENHEGV
277
RRFDEILEAS
287
DGIMVARGDL
297
GIEIPAEKVF
307
LAQKMMIGRC
317

NRAGKPVICA
327
TQMLESMIKK
337
PRPTRAEGSD
347
VANAVLDGAD
357
CIMLSGETAK
367

GDYPLEAVRM
377
QHLIAREAEA
387
AIYHLQLFEE
397
LRRLAPITSD
407
PTEATAVGAV
417

EASFKCCSGA
427
IIVLTKSGRS
437
AHQVARYRPR
447
APIIAVTRNP
457
QTARQAHLYR
467

GIFPVLCKDP
477
VQEAWAEDVD
487
LRVNFAMNVG
497
KARGFFKKGD
507
VVIVLTGWRP
517

GSGFTNTMRV
527
VPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:455 or .A:482 or .A:485 or .A:486 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.392
THR432
2.681
LYS433
3.401
SER434
2.907
GLY435
3.866
ARG436
3.348
SER437
2.860
ALA438
4.755
ARG455
4.838
TRP482
3.497
ASP485
4.338
VAL486
4.682
Residue
Distance (Å)
ARG489
2.744
THR513
4.115
GLY514
3.122
TRP515
4.068
ARG516
2.724
PRO517
3.779
GLY518
2.975
SER519
3.044
GLY520
3.016
PHE521
2.957
THR522
3.752
PDB ID: 3GR4      Activator-Bound Structure of Human Pyruvate Kinase M2
Method X-ray diffraction Resolution 1.60 Å Mutation No [6]
PDB Sequence
IQTQQLHAAM
22
ADTFLEHMCR
32
LDIDSPPITA
42
RNTGIICTIG
52
PASRSVETLK
62

EMIKSGMNVA
72
RLNFSHGTHE
82
YHAETIKNVR
92
TATESFASDP
102
ILYRPVAVAL
112

DTKGPEIRTG
122
LIKGSGTAEV
132
ELKKGATLKI
142
TLDNAYMEKC
152
DENILWLDYK
162

NICKVVEVGS
172
KIYVDDGLIS
182
LQVKQKGADF
192
LVTEVENGGS
202
LGSKKGVNLP
212

GAAVDLPAVS
222
EKDIQDLKFG
232
VEQDVDMVFA
242
SFIRKASDVH
252
EVRKVLGEKG
262

KNIKIISKIE
272
NHEGVRRFDE
282
ILEASDGIMV
292
ARGDLGIEIP
302
AEKVFLAQKM
312

MIGRCNRAGK
322
PVICATQMLE
332
SMIKKPRPTR
342
AEGSDVANAV
352
LDGADCIMLS
362

GETAKGDYPL
372
EAVRMQHLIA
382
REAEAAIYHL
392
QLFEELRRLA
402
PITSDPTEAT
412

AVGAVEASFK
422
CCSGAIIVLT
432
KSGRSAHQVA
442
RYRPRAPIIA
452
VTRNPQTARQ
462

AHLYRGIFPV
472
LCKDPVQEAW
482
AEDVDLRVNF
492
AMNVGKARGF
502
FKKGDVVIVL
512

TGWRPGSGFT
522
NTMRVVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:485 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.772
THR432
2.515
LYS433
3.149
SER434
2.536
GLY435
4.028
ARG436
3.764
SER437
2.713
ALA438
4.854
TRP482
2.708
ASP485
4.620
ARG489
2.870
Residue
Distance (Å)
THR513
4.140
GLY514
2.994
TRP515
3.884
ARG516
2.605
PRO517
3.625
GLY518
2.625
SER519
2.702
GLY520
2.848
PHE521
2.841
THR522
3.410
PDB ID: 3GQY      Activator-Bound Structure of Human Pyruvate Kinase M2
Method X-ray diffraction Resolution 1.85 Å Mutation No [7]
PDB Sequence
QTQQLHAAMA
23
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63

MIKSGMNVAR
73
LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113

TKGPEIRTGL
123
IKGSGTAEVE
133
LKKGATLKIT
143
LDNAYMEKCD
153
ENILWLDYKN
163

ICKVVEVGSK
173
IYVDDGLISL
183
QVADFLVTEV
197
ENGGSLGSKK
207
GVNLPGAAVD
217

LPAVSEKDIQ
227
DLKFGVEQDV
237
DMVFASFIRK
247
ASDVHEVRKV
257
LGEKGKNIKI
267

ISKIENHEGV
277
RRFDEILEAS
287
DGIMVARGDL
297
GIEIPAEKVF
307
LAQKMMIGRC
317

NRAGKPVICA
327
TQMLESMIKK
337
PRPTRAEGSD
347
VANAVLDGAD
357
CIMLSGETAK
367

GDYPLEAVRM
377
QHLIAREAEA
387
AIYHLQLFEE
397
LRRLAPITSD
407
PTEATAVGAV
417

EASFKCCSGA
427
IIVLTKSGRS
437
AHQVARYRPR
447
APIIAVTRNP
457
QTARQAHLYR
467

GIFPVLCKDP
477
VQEAWAEDVD
487
LRVNFAMNVG
497
KARGFFKKGD
507
VVIVLTGWRP
517

GSGFTNTMRV
527
VPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:485 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.711
THR432
2.528
LYS433
3.196
SER434
2.636
GLY435
4.026
ARG436
3.749
SER437
2.667
ALA438
4.906
TRP482
2.795
ASP485
4.456
ARG489
2.772
Residue
Distance (Å)
THR513
4.023
GLY514
2.914
TRP515
3.923
ARG516
2.692
PRO517
3.814
GLY518
2.646
SER519
2.779
GLY520
2.774
PHE521
2.801
THR522
3.354
PDB ID: 3ME3      Activator-Bound Structure of Human Pyruvate Kinase M2
Method X-ray diffraction Resolution 1.95 Å Mutation No [1]
PDB Sequence
QTQQLHAAMA
23
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63

MIKSGMNVAR
73
LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113

TKGPEIRTGL
123
IKGSGTAEVE
133
LKKGATLKIT
143
LDNAYMEKCD
153
ENILWLDYKN
163

ICKVVEVGSK
173
IYVDDGLISL
183
QVKQKGADFL
193
VTEVENGGSL
203
GSKKGVNLPG
213

AAVDLPAVSE
223
KDIQDLKFGV
233
EQDVDMVFAS
243
FIRKASDVHE
253
VRKVLGEKGK
263

NIKIISKIEN
273
HEGVRRFDEI
283
LEASDGIMVA
293
RGDLGIEIPA
303
EKVFLAQKMM
313

IGRCNRAGKP
323
VICATQMLES
333
MIKKPRPTRA
343
EGSDVANAVL
353
DGADCIMLSG
363

ETAKGDYPLE
373
AVRMQHLIAR
383
EAEAAIYHLQ
393
LFEELRRLAP
403
ITSDPTEATA
413

VGAVEASFKC
423
CSGAIIVLTK
433
SGRSAHQVAR
443
YRPRAPIIAV
453
TRNPQTARQA
463

HLYRGIFPVL
473
CKDPVQEAWA
483
EDVDLRVNFA
493
MNVGKARGFF
503
KKGDVVIVLT
513

GWRPGSGFTN
523
TMRVVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:485 or .A:486 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.598
THR432
2.511
LYS433
3.194
SER434
2.660
GLY435
4.119
ARG436
3.782
SER437
2.741
ALA438
4.877
TRP482
2.732
ASP485
4.709
VAL486
4.919
Residue
Distance (Å)
ARG489
2.729
THR513
3.957
GLY514
2.852
TRP515
3.901
ARG516
2.938
PRO517
3.652
GLY518
2.716
SER519
2.648
GLY520
2.925
PHE521
2.854
THR522
3.375
PDB ID: 3H6O      Activator-Bound Structure of Human Pyruvate Kinase M2
Method X-ray diffraction Resolution 2.00 Å Mutation No [8]
PDB Sequence
QTQQLHAAMA
23
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63

MIKSGMNVAR
73
LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113

TKGPEIRTGI
142
TLCDENILWL
159
DYKNICKVVE
169
VGSKIYVDDG
179
LISLQVKQKG
189

ADFLVTEVEN
199
GGGSKKGVNL
211
PGAAVDLPAV
221
SEKDIQDLKF
231
GVEQDVDMVF
241

ASFIRKASDV
251
HEVRKVLGEK
261
GKNIKIISKI
271
ENHEGVRRFD
281
EILEASDGIM
291

VARGDLGIEI
301
PAEKVFLAQK
311
MMIGRCNRAG
321
KPVICATQML
331
ESMIKKPRPT
341

RAEGSDVANA
351
VLDGADCIML
361
SGETAKGDYP
371
LEAVRMQHLI
381
AREAEAAIYH
391

LQLFEELRRL
401
APITSDPTEA
411
TAVGAVEASF
421
KCCSGAIIVL
431
TKSGRSAHQV
441

ARYRPRAPII
451
AVTRNPQTAR
461
QAHLYRGIFP
471
VLCKDPVQEA
481
WAEDVDLRVN
491

FAMNVGKARG
501
FFKKGDVVIV
511
LTGWRPGSGF
521
TNTMRVVPVP
531
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:482 or .A:485 or .A:486 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.474
THR432
2.707
LYS433
3.138
SER434
2.506
GLY435
4.259
ARG436
3.748
SER437
2.798
TRP482
2.882
ASP485
4.410
VAL486
4.927
ARG489
2.951
Residue
Distance (Å)
THR513
4.135
GLY514
3.125
TRP515
4.044
ARG516
2.651
PRO517
3.752
GLY518
2.540
SER519
2.728
GLY520
2.654
PHE521
2.975
THR522
3.535
PDB ID: 5X1V      PKM2 in complex with compound 2
Method X-ray diffraction Resolution 2.10 Å Mutation No [9]
PDB Sequence
QTQQLHAAMA
23
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63

MIKSGMNVAR
73
LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113

TKGPEIRTGL
123
IKGSGTAEVE
133
LKKGATLKIT
143
LDNAYMEKCD
153
ENILWLDYKN
163

ICKVVEVGSK
173
IYVDDGLISL
183
QVKLVTEVEN
199
GGSLGSKKGV
209
NLPGAAVDLP
219

AVSEKDIQDL
229
KFGVEQDVDM
239
VFASFIRKAS
249
DVHEVRKVLG
259
EKGKNIKIIS
269

KIENHEGVRR
279
FDEILEASDG
289
IMVARGDLGI
299
EIPAEKVFLA
309
QKMMIGRCNR
319

AGKPVICATQ
329
MLESMIKKPR
339
PTRAEGSDVA
349
NAVLDGADCI
359
MLSGETAKGD
369

YPLEAVRMQH
379
LIAREAEAAI
389
YHLQLFEELR
399
RLAPITSDPT
409
EATAVGAVEA
419

SFKCCSGAII
429
VLTKSGRSAH
439
QVARYRPRAP
449
IIAVTRNPQT
459
ARQAHLYRGI
469

FPVLCKDPVQ
479
EAWAEDVDLR
489
VNFAMNVGKA
499
RGFFKKGDVV
509
IVLTGWRPGS
519

GFTNTMRVVP
529
VP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:485 or .A:486 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.618
THR432
2.478
LYS433
2.874
SER434
2.701
GLY435
4.271
ARG436
3.663
SER437
2.819
ALA438
4.906
TRP482
2.611
ASP485
4.784
VAL486
4.796
Residue
Distance (Å)
ARG489
2.747
THR513
4.162
GLY514
3.302
TRP515
4.276
ARG516
2.923
PRO517
3.443
GLY518
2.577
SER519
2.399
GLY520
2.795
PHE521
3.021
THR522
3.495
PDB ID: 6WP5      Pyruvate Kinase M2 mutant-S37D
Method X-ray diffraction Resolution 2.17 Å Mutation Yes [10]
PDB Sequence
AMADTFLEHM
30
CRLDIDDPPI
40
TARNTGIICT
50
IGPASRSVET
60
LKEMIKSGMN
70

VARLNFSHGT
80
HEYHAETIKN
90
VRTATESFAS
100
DPILYRPVAV
110
ALDTKGPEIR
120

TGLIKGSGAE
131
VELKKGATLK
141
ITLDNAYMEK
151
CDENILWLDY
161
KNICKVVEVG
171

SKIYVDDGLI
181
SLQVKQKGAD
191
FLVTEVENGG
201
SLGSKKGVNL
211
PGAAVDLPAV
221

SEKDIQDLKF
231
GVEQDVDMVF
241
ASFIRKASDV
251
HEVRKVLGEK
261
GKNIKIISKI
271

ENHEGVRRFD
281
EILEASDGIM
291
VARGDLGIEI
301
PAEKVFLAQK
311
MMIGRCNRAG
321

KPVICATQML
331
ESMIKKPRPT
341
RAEGSDVANA
351
VLDGADCIML
361
SGETAKGDYP
371

LEAVRMQHLI
381
AREAEAAIYH
391
LQLFEELRRL
401
APITSDPTEA
411
TAVGAVEASF
421

KCCSGAIIVL
431
TKSGRSAHQV
441
ARYRPRAPII
451
AVTRNPQTAR
461
QAHLYRGIFP
471

VLCKDPVQEA
481
WAEDVDLRVN
491
FAMNVGKARG
501
FFKKGDVVIV
511
LTGWRPGSGF
521

TNTMRVVPVP
531
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .B:431 or .B:432 or .B:433 or .B:434 or .B:435 or .B:436 or .B:437 or .B:438 or .B:518 or .B:519 or .B:520 or .B:521 or .B:522; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
4.460
THR432
2.647
LYS433
3.206
SER434
2.387
GLY435
3.760
ARG436
3.949
SER437
2.344
Residue
Distance (Å)
ALA438
4.919
GLY518
3.984
SER519
2.809
GLY520
2.674
PHE521
4.415
THR522
4.154
PDB ID: 7L21      Pyruvate Kinase M2 mutant-N70D
Method X-ray diffraction Resolution 2.29 Å Mutation Yes [11]
PDB Sequence
IQTQQLHAAM
22
ADTFLEHMCR
32
LDIDSPPITA
42
RNTGIICTIG
52
PASRSVETLK
62

EMIKSGMDVA
72
RLNFSHGTHE
82
YHAETIKNVR
92
TATESFASDP
102
ILYRPVAVAL
112

DTKGPEIRTG
122
LIKGGTAEVE
133
LKKGATLKIT
143
LDNAYMEKCD
153
ENILWLDYKN
163

ICKVVEVGSK
173
IYVDDGLISL
183
QVKQKGADFL
193
VTEVENGGSL
203
GSKKGVNLPG
213

AAVDLPAVSE
223
KDIQDLKFGV
233
EQDVDMVFAS
243
FIRKASDVHE
253
VRKVLGEKGK
263

NIKIISKIEN
273
HEGVRRFDEI
283
LEASDGIMVA
293
RGDLGIEIPA
303
EKVFLAQKMM
313

IGRCNRAGKP
323
VICATQMLES
333
MIKKPRPTRA
343
EGSDVANAVL
353
DGADCIMLSG
363

ETAKGDYPLE
373
AVRMQHLIAR
383
EAEAAIYHLQ
393
LFEELRRLPI
404
TSDPTEATAV
414

GAVEASFKCC
424
SGAIIVLTKS
434
GRSAHQVARY
444
RPRAPIIAVT
454
RNPQTARQAH
464

LYRGIFPVLC
474
KDPVQEAWAE
484
DVDLRVNFAM
494
NVGKARGFFK
504
KGDVVIVLTG
514

WRPGFTNTMR
526
VVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:489 or .A:521 or .A:522; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.456
THR432
2.479
LYS433
2.878
SER434
2.377
GLY435
3.869
ARG436
3.587
Residue
Distance (Å)
SER437
2.654
ALA438
4.889
TRP482
4.791
ARG489
4.205
PHE521
3.825
THR522
3.827
PDB ID: 6V74      Crystal Structure of Human PKM2 in Complex with L-asparagine
Method X-ray diffraction Resolution 2.32 Å Mutation No [12]
PDB Sequence
QTQQLHAAMA
23
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63

MIKSGMNVAR
73
LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113

TKGPEIRTGL
123
IKGVELKKGA
138
TLKITLDNAY
148
MEKCDENILW
158
LDYKNICKVV
168

EVGSKIYVDD
178
GLISLQVKQK
188
GADFLVTEVE
198
NGGSLGSKKG
208
VNLPGAAVDL
218

PAVSEKDIQD
228
LKFGVEQDVD
238
MVFASFIRKA
248
SDVHEVRKVL
258
GEKGKNIKII
268

SKIENHEGVR
278
RFDEILEASD
288
GIMVARGDLG
298
IEIPAEKVFL
308
AQKMMIGRCN
318

RAGKPVICAT
328
QMLESMIKKP
338
RPTRAEGSDV
348
ANAVLDGADC
358
IMLSGETAKG
368

DYPLEAVRMQ
378
HLIAREAEAA
388
IYHLQLFEEL
398
RRLAPITSDP
408
TEATAVGAVE
418

ASFKCCSGAI
428
IVLTKSGRSA
438
HQVARYRPRA
448
PIIAVTRNPQ
458
TARQAHLYRG
468

IFPVLCKDPV
478
QEAWAEDVDL
488
RVNFAMNVGK
498
ARGFFKKGDV
508
VIVLTGWRPG
518

SGFTNTMRVV
528
PVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:485 or .A:486 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.433
THR432
2.504
LYS433
3.120
SER434
2.843
GLY435
4.065
ARG436
3.651
SER437
2.442
ALA438
4.827
TRP482
2.739
ASP485
4.444
VAL486
4.866
Residue
Distance (Å)
ARG489
2.621
THR513
4.139
GLY514
2.997
TRP515
4.055
ARG516
3.002
PRO517
3.516
GLY518
2.354
SER519
2.671
GLY520
2.788
PHE521
3.029
THR522
3.246
PDB ID: 6V76      Crystal Structure of Human PKM2 in Complex with L-valine
Method X-ray diffraction Resolution 2.75 Å Mutation No [12]
PDB Sequence
HAAMADTFLE
28
HMCRLDIDSP
38
PITARNTGII
48
CTIGPASRSV
58
ETLKEMIKSG
68

MNVARLNFSH
78
GTHEYHAETI
88
KNVRTATESF
98
ASDPILYRPV
108
AVALDTKGPE
118

IRTGLIKGSG
128
TAEVELKKGA
138
TLKITLDNAY
148
MEKCDENILW
158
LDYKNICKVV
168

EVGSKIYVDD
178
GLISLQVKQK
188
GALVTEVENG
200
GSLGSKKGVN
210
LPGAAVDLPA
220

VSEKDIQDLK
230
FGVEQDVDMV
240
FASFIRKASD
250
VHEVRKVLGE
260
KGKNIKIISK
270

IENHEGVRRF
280
DEILEASDGI
290
MVARGDLGIE
300
IPAEKVFLAQ
310
KMMIGRCNRA
320

GKPVICATQM
330
LESMIKKPRP
340
TRAEGSDVAN
350
AVLDGADCIM
360
LSGETAKGDY
370

PLEAVRMQHL
380
IAREAEAAIY
390
HLQLFEELRR
400
LAPITSDPTE
410
ATAVGAVEAS
420

FKCCSGAIIV
430
LTKSGRSAHQ
440
VARYRPRAPI
450
IAVTRNPQTA
460
RQAHLYRGIF
470

PVLCKDPVQE
480
AWAEDVDLRV
490
NFAMNVGKAR
500
GFFKKGDVVI
510
VLTGWRPGSG
520

FTNTMRVVPV
530
P
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .C:431 or .C:432 or .C:433 or .C:434 or .C:435 or .C:436 or .C:437 or .C:438 or .C:482 or .C:485 or .C:486 or .C:489 or .C:513 or .C:514 or .C:515 or .C:516 or .C:517 or .C:518 or .C:519 or .C:520 or .C:521 or .C:522; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.485
THR432
2.334
LYS433
3.109
SER434
3.119
GLY435
3.749
ARG436
3.360
SER437
2.932
ALA438
4.857
TRP482
3.067
ASP485
4.193
VAL486
4.756
Residue
Distance (Å)
ARG489
2.327
THR513
3.997
GLY514
2.971
TRP515
4.021
ARG516
3.135
PRO517
3.246
GLY518
2.327
SER519
2.563
GLY520
2.403
PHE521
3.346
THR522
3.169
PDB ID: 6V75      Crystal Structure of Human PKM2 in Complex with L-aspartate
Method X-ray diffraction Resolution 2.85 Å Mutation No [12]
PDB Sequence
TQQLHAAMAD
24
TFLEHMCRLD
34
IDSPPITARN
44
TGIICTIGPA
54
SRSVETLKEM
64

IKSGMNVARL
74
NFSHGTHEYH
84
AETIKNVRTA
94
TESFASDPIL
104
YRPVAVALDT
114

KGPEIRTGLI
124
KGSGTAEVEL
134
KKGATLKITL
144
DNAYMEKCDE
154
NILWLDYKNI
164

CKVVEVGSKI
174
YVDDGLISLQ
184
VKQKGADFLV
194
TEVENGGSLG
204
SKKGVNLPGA
214

AVDLPAVSEK
224
DIQDLKFGVE
234
QDVDMVFASF
244
IRKASDVHEV
254
RKVLGEKGKN
264

IKIISKIENH
274
EGVRRFDEIL
284
EASDGIMVAR
294
GDLGIEIPAE
304
KVFLAQKMMI
314

GRCNRAGKPV
324
ICATQMLESM
334
IKKPRPTRAE
344
GSDVANAVLD
354
GADCIMLSGE
364

TAKGDYPLEA
374
VRMQHLIARE
384
AEAAIYHLQL
394
FEELRRLAPI
404
TSDPTEATAV
414

GAVEASFKCC
424
SGAIIVLTKS
434
GRSAHQVARY
444
RPRAPIIAVT
454
RNPQTARQAH
464

LYRGIFPVLC
474
KDPVQEAWAE
484
DVDLRVNFAM
494
NVGKARGFFK
504
KGDVVIVLTG
514

WRPGSGFTNT
524
MRVVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .C:431 or .C:432 or .C:433 or .C:434 or .C:435 or .C:436 or .C:437 or .C:455 or .C:482 or .C:485 or .C:489 or .C:513 or .C:514 or .C:516 or .C:517 or .C:518 or .C:519 or .C:520 or .C:521 or .C:522; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.850
THR432
2.597
LYS433
3.443
SER434
3.022
GLY435
4.393
ARG436
4.114
SER437
3.157
ARG455
4.671
TRP482
3.719
ASP485
4.185
Residue
Distance (Å)
ARG489
1.696
THR513
4.133
GLY514
3.257
ARG516
3.362
PRO517
3.467
GLY518
2.324
SER519
3.092
GLY520
2.354
PHE521
2.974
THR522
3.971
PDB ID: 5X1W      PKM2 in complex with compound 5
Method X-ray diffraction Resolution 3.00 Å Mutation No [9]
PDB Sequence
QTQQLHAAMA
23
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63

MIKSGMNVAR
73
LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113

TKGPEIRTGL
123
IKGSGTAEVE
133
LKKGATLKIT
143
LDNAYMEKCD
153
ENILWLDYKN
163

ICKVVEVGSK
173
IYVDDGLISL
183
QVKQKGADFL
193
VTEVENGGSL
203
GSKKGVNLPG
213

AAVDLPAVSE
223
KDIQDLKFGV
233
EQDVDMVFAS
243
FIRKASDVHE
253
VRKVLGEKGK
263

NIKIISKIEN
273
HEGVRRFDEI
283
LEASDGIMVA
293
RGDLGIEIPA
303
EKVFLAQKMM
313

IGRCNRAGKP
323
VICATQMLES
333
MIKKPRPTRA
343
EGSDVANAVL
353
DGADCIMLSG
363

ETAKGDYPLE
373
AVRMQHLIAR
383
EAEAAIYHLQ
393
LFEELRRLAP
403
ITSDPTEATA
413

VGAVEASFKC
423
CSGAIIVLTK
433
SGRSAHQVAR
443
YRPRAPIIAV
453
TRNPQTARQA
463

HLYRGIFPVL
473
CKDPVQEAWA
483
EDVDLRVNFA
493
MNVGKARGFF
503
KKGDVVIVLT
513

GWRPGSGFTN
523
TMRVVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:485 or .A:486 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.467
THR432
2.403
LYS433
3.172
SER434
2.701
GLY435
4.197
ARG436
3.778
SER437
2.476
ALA438
4.935
TRP482
2.620
ASP485
4.742
VAL486
4.911
Residue
Distance (Å)
ARG489
2.758
THR513
4.247
GLY514
3.238
TRP515
4.281
ARG516
3.146
PRO517
3.370
GLY518
2.591
SER519
2.617
GLY520
2.819
PHE521
3.131
THR522
3.344
PDB ID: 6NU1      Crystal Structure of Human PKM2 in Complex with L-cysteine
Method X-ray diffraction Resolution 2.25 Å Mutation No [13]
PDB Sequence
QTQQLHAAMA
23
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63

MIKSGMNVAR
73
LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113

TKGPEIRTEV
132
ELKKKITLCD
153
ENILWLDYKN
163
ISKIYVDDGL
180
ISLENGGSLG
204

KKGVNLPGAA
215
VDLPAVSEKD
225
IQDLKFGVEQ
235
DVDMVFASFI
245
RKASDVHEVR
255

KVLGEKGKNI
265
KIISKIENHE
275
GVRRFDEILE
285
ASDGIMVARG
295
DLGIEIPAEK
305

VFLAQKMMIG
315
RCNRAGKPVI
325
CATQMLESMI
335
KKPRPTRAEG
345
SDVANAVLDG
355

ADCIMLSGET
365
AKGDYPLEAV
375
RMQHLIAREA
385
EAAIYHLQLF
395
EELRRLAPIT
405

SDPTEATAVG
415
AVEASFKCCS
425
GAIIVLTKSG
435
RSAHQVARYR
445
PRAPIIAVTR
455

NPQTARQAHL
465
YRGIFPVLCK
475
DPVQEAWAED
485
VDLRVNFAMN
495
VGKARGFFKK
505

GDVVIVLTGW
515
RPGSGFTNTM
525
RVVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.465
THR432
2.547
LYS433
3.122
SER434
2.456
GLY435
3.907
ARG436
3.709
SER437
2.877
ALA438
4.760
TRP482
3.142
ARG489
2.748
Residue
Distance (Å)
THR513
4.253
GLY514
2.964
TRP515
3.855
ARG516
3.076
PRO517
3.450
GLY518
2.425
SER519
3.111
GLY520
2.815
PHE521
2.988
THR522
3.466
PDB ID: 4FXF      Structure of M2 pyruvate kinase in complex with phenylalanine
Method X-ray diffraction Resolution 2.55 Å Mutation No [14]
PDB Sequence
CRLDIDSPPI
40
TARNTGIICT
50
IGPASRSVET
60
LKEMIKSGMN
70
VARLNFSHGT
80

HEYHAETIKN
90
VRTATESFAS
100
DPILYRPVAV
110
ALDTKGPEIR
120
TGLIKGSGTA
130

EVELKKGATL
140
KITLDNAYME
150
KCDENILWLD
160
YKNICKVVEV
170
GSKIYVDDGL
180

ISLQVKQKGA
190
DFLVTEVENG
200
GSLGSKKGVN
210
LPGAAVDLPA
220
VSEKDIQDLK
230

FGVEQDVDMV
240
FASFIRKASD
250
VHEVRKVLGE
260
KGKNIKIISK
270
IENHEGVRRF
280

DEILEASDGI
290
MVARGDLGIE
300
IPAEKVFLAQ
310
KMMIGRCNRA
320
GKPVICATQM
330

LESMIKKPRP
340
TRAEGSDVAN
350
AVLDGADCIM
360
LSGETAKGDY
370
PLEAVRMQNL
380

IAREAEAAIY
390
HLQLFEELRR
400
LAPITSDPTE
410
ATAVGAVEAS
420
FKCCSGAIIV
430

LTKSGRSAHQ
440
VARYRPRAPI
450
IAVTRNPQTA
460
RQAHLYRGIF
470
PVLCKDPVQE
480

AWAEDVDLRV
490
NFAMNVGKAR
500
GFFKKGDVVI
510
VLTGWRPGSG
520
FTNTMRVVPV
530

P
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:485 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.349
THR432
2.591
LYS433
3.063
SER434
2.709
GLY435
4.074
ARG436
3.707
SER437
2.734
ALA438
4.892
TRP482
2.909
ASP485
4.862
ARG489
2.938
Residue
Distance (Å)
THR513
4.176
GLY514
2.916
TRP515
3.928
ARG516
2.994
PRO517
3.435
GLY518
2.529
SER519
2.894
GLY520
2.717
PHE521
2.835
THR522
3.338
PDB ID: 5X0I      Crystal structure of PKM2 R399E mutant complexed with FBP and serine
Method X-ray diffraction Resolution 2.64 Å Mutation Yes [15]
PDB Sequence
QTQQLHAAMA
23
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63

MIKSGMNVAR
73
LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113

TKGPEIRTGL
123
IKGSGTAEVE
133
LKKGATLKIT
143
LDNAYMEKCD
153
ENILWLDYKN
163

ICKVVEVGSK
173
IYVDDGLISL
183
QVKQKGADFL
193
VTEVENGGSL
203
GSKKGVNLPG
213

AAVDLPAVSE
223
KDIQDLKFGV
233
EQDVDMVFAS
243
FIRKASDVHE
253
VRKVLGEKGK
263

NIKIISKIEN
273
HEGVRRFDEI
283
LEASDGIMVA
293
RGDLGIEIPA
303
EKVFLAQKMM
313

IGRCNRAGKP
323
VICATQMLES
333
MIKKPRPTRA
343
EGSDVANAVL
353
DGADCIMLSG
363

ETAKGDYPLE
373
AVRMQHLIAR
383
EAEAAIYHLQ
393
LFEELERLAP
403
ITSDPTEATA
413

VGAVEASFKC
423
CSGAIIVLTK
433
SGRSAHQVAR
443
YRPRAPIIAV
453
TRNPQTARQA
463

HLYRGIFPVL
473
CKDPVQEAWA
483
EDVDLRVNFA
493
MNVGKARGFF
503
KKGDVVIVLT
513

GWRPGSGFTN
523
TMRVVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:455 or .A:482 or .A:485 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.608
THR432
2.504
LYS433
3.223
SER434
2.837
GLY435
4.138
ARG436
3.719
SER437
2.333
ALA438
4.804
ARG455
4.842
TRP482
2.683
ASP485
4.360
Residue
Distance (Å)
ARG489
2.765
THR513
4.083
GLY514
2.930
TRP515
4.015
ARG516
2.835
PRO517
3.313
GLY518
2.636
SER519
2.478
GLY520
2.731
PHE521
2.647
THR522
3.271
PDB ID: 4WJ8      Human Pyruvate Kinase M2 Mutant C424A
Method X-ray diffraction Resolution 2.87 Å Mutation Yes [16]
PDB Sequence
QTQQLHAAMA
23
DTFLEHMCRL
33
DIDSPPITAR
43
NTGIICTIGP
53
ASRSVETLKE
63

MIKSGMNVAR
73
LNFSHGTHEY
83
HAETIKNVRT
93
ATESFASDPI
103
LYRPVAVALD
113

TKGPEIRTGL
123
IKGSGTAEVE
133
LKKGATLKIT
143
LDNAYMEKCD
153
ENILWLDYKN
163

ICKVVEVGSK
173
IYVDDGLISL
183
QVKQKGADFL
193
VTEVENGGSL
203
GSKKGVNLPG
213

AAVDLPAVSE
223
KDIQDLKFGV
233
EQDVDMVFAS
243
FIRKASDVHE
253
VRKVLGEKGK
263

NIKIISKIEN
273
HEGVRRFDEI
283
LEASDGIMVA
293
RGDLGIEIPA
303
EKVFLAQKMM
313

IGRCNRAGKP
323
VICATQMLES
333
MIKKPRPTRA
343
EGSDVANAVL
353
DGADCIMLSG
363

ETAKGDYPLE
373
AVRMQHLIAR
383
EAEAAIYHLQ
393
LFEELRRLAP
403
ITSDPTEATA
413

VGAVEASFKC
423
ASGAIIVLTK
433
SGRSAHQVAR
443
YRPRAPIIAV
453
TRNPQTARQA
463

HLYRGIFPVL
473
CKDPVQEAWA
483
EDVDLRVNFA
493
MNVGKARGFF
503
KKGDVVIVLT
513

GWRPGSGFTN
523
TMRVVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:485 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
2.984
THR432
2.679
LYS433
3.249
SER434
2.739
GLY435
3.927
ARG436
3.454
SER437
2.760
ALA438
4.714
TRP482
3.805
ASP485
4.840
ARG489
3.303
Residue
Distance (Å)
THR513
3.849
GLY514
2.712
TRP515
4.632
ARG516
3.074
PRO517
3.430
GLY518
2.565
SER519
2.896
GLY520
2.963
PHE521
3.160
THR522
3.141
PDB ID: 3SRD      Human M2 pyruvate kinase in complex with fructose 1-6 bisphosphate and Oxalate.
Method X-ray diffraction Resolution 2.90 Å Mutation No [17]
PDB Sequence
IQTQQLHAAM
22
ADTFLEHMCR
32
LDIDSPPITA
42
RNTGIICTIG
52
PASRSVETLK
62

EMIKSGMNVA
72
RLNFSHGTHE
82
YHAETIKNVR
92
TATESFASDP
102
ILYRPVAVAL
112

DTKGPEIRTG
122
LIKGEVELKK
136
GATLKITLDN
146
AYMEKCDENI
156
LWLDYKNICK
166

VVEVGSKIYV
176
DDGLISLQVK
186
QKGADFLVTE
196
VENGGSLGSK
206
KGVNLPGAAV
216

DLPAVSEKDI
226
QDLKFGVEQD
236
VDMVFASFIR
246
KASDVHEVRK
256
VLGEKGKNIK
266

IISKIENHEG
276
VRRFDEILEA
286
SDGIMVARGD
296
LGIEIPAEKV
306
FLAQKMMIGR
316

CNRAGKPVIC
326
ATQMLESMIK
336
KPRPTRAEGS
346
DVANAVLDGA
356
DCIMLSGETA
366

KGDYPLEAVR
376
MQHLIAREAE
386
AAIYHLQLFE
396
ELRRLAPITS
406
DPTEATAVGA
416

VEASFKCCSG
426
AIIVLTKSGR
436
SAHQVARYRP
446
RAPIIAVTRN
456
PQTARQAHLY
466

RGIFPVLCKD
476
PVQEAWAEDV
486
DLRVNFAMNV
496
GKARGFFKKG
506
DVVIVLTGWR
516

PGSGFTNTMR
526
VVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:482 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.565
THR432
2.594
LYS433
3.222
SER434
3.050
GLY435
4.183
ARG436
3.866
SER437
2.789
TRP482
2.622
ARG489
3.057
THR513
4.016
Residue
Distance (Å)
GLY514
2.883
TRP515
3.957
ARG516
2.681
PRO517
3.246
GLY518
2.404
SER519
2.768
GLY520
2.656
PHE521
2.941
THR522
3.046
PDB ID: 4JPG      2-((1H-benzo[d]imidazol-1-yl)methyl)-4H-pyrido[1,2-a]pyrimidin-4-ones as Novel PKM2 Activators
Method X-ray diffraction Resolution 2.33 Å Mutation No [18]
PDB Sequence
IQTQQLHAAM
22
ADTFLEHMCR
32
LDIDSPPITA
42
RNTGIICTIG
52
PASRSVETLK
62

EMIKSGMNVA
72
RLNFSHGTHE
82
YHAETIKNVR
92
TATESFASDP
102
ILYRPVAVAL
112

DTKGPEIRTG
122
LIKGSGTAEV
132
ELKKGATLKI
142
TLDNAYMEKC
152
DENILWLDYK
162

NICKVVEVGS
172
KIYVDDGLIS
182
LQVKQKGADF
192
LVTEVENGGS
202
LGSKKGVNLP
212

GAAVDLPAVS
222
EKDIQDLKFG
232
VEQDVDMVFA
242
SFIRKASDVH
252
EVRKVLGEKG
262

KNIKIISKIE
272
NHEGVRRFDE
282
ILEASDGIMV
292
ARGDLGIEIP
302
AEKVFLAQKM
312

MIGRCNRAGK
322
PVICATQMLE
332
SMIKKPRPTR
342
AEGSDVANAV
352
LDGADCIMLS
362

GETAKGDYPL
372
EAVRMQHLIA
382
REAEAAIYHL
392
QLFEELRRLA
402
PITSDPTEAT
412

AVGAVEASFK
422
CCSGAIIVLT
432
KSGRSAHQVA
442
RYRPRAPIIA
452
VTRNPQTARQ
462

AHLYRGIFPV
472
LCKDPVQEAW
482
AEDVDLRVNF
492
AMNVGKARGF
502
FKKGDVVIVL
512

TGWRPGSGFT
522
NTMRVVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:485 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.460
THR432
2.662
LYS433
3.181
SER434
2.688
GLY435
4.103
ARG436
3.846
SER437
2.626
ALA438
4.953
TRP482
2.761
ASP485
4.630
ARG489
2.778
Residue
Distance (Å)
THR513
4.025
GLY514
2.984
TRP515
3.976
ARG516
2.728
PRO517
3.489
GLY518
2.666
SER519
2.834
GLY520
2.805
PHE521
2.899
THR522
3.371
PDB ID: 1T5A      Human Pyruvate Kinase M2
Method X-ray diffraction Resolution 2.80 Å Mutation No [19]
PDB Sequence
IQTQQLHAAM
22
ADTFLEHMCR
32
LDIDSPPITA
42
RNTGIICTIG
52
PASRSVETLK
62

EMIKSGMNVA
72
RLNFSHGTHE
82
YHAETIKNVR
92
TATESFASDP
102
ILYRPVAVAL
112

DTKGPEIRTG
122
LIKGSGTAEV
132
ELKKGATLKI
142
TLDNAYMEKC
152
DENILWLDYK
162

NICKVVEVGS
172
KIYVDDGLIS
182
LQVKQKGADF
192
LVTEVENGGS
202
LGSKKGVNLP
212

GAAVDLPAVS
222
EKDIQDLKFG
232
VEQDVDMVFA
242
SFIRKASDVH
252
EVRKVLGEKG
262

KNIKIISKIE
272
NHEGVRRFDE
282
ILEASDGIMV
292
ARGDLGIEIP
302
AEKVFLAQKM
312

MIGRCNRAGK
322
PVICATQMLE
332
SMIKKPRPTR
342
AEGSDVANAV
352
LDGADCIMLS
362

GETAKGDYPL
372
EAVRMQNLIA
382
REAEAAIYHL
392
QLFEELRRLA
402
PITSDPTEAT
412

AVGAVEASFK
422
CCSGAIIVLT
432
KSGRSAHQVA
442
RYRPRAPIIA
452
VTRNPQTARQ
462

AHLYRGIFPV
472
LCKDPVQEAW
482
AEDVDLRVNF
492
AMNVGKARGF
502
FKKGDVVIVL
512

TGWRPGSGFT
522
NTMRVVPVP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FBP or .FBP2 or .FBP3 or :3FBP;style chemicals stick;color identity;select .A:431 or .A:432 or .A:433 or .A:434 or .A:435 or .A:436 or .A:437 or .A:438 or .A:482 or .A:485 or .A:486 or .A:489 or .A:513 or .A:514 or .A:515 or .A:516 or .A:517 or .A:518 or .A:519 or .A:520 or .A:521 or .A:522; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU431
3.173
THR432
2.537
LYS433
2.700
SER434
3.022
GLY435
4.202
ARG436
4.092
SER437
2.603
ALA438
4.955
TRP482
2.862
ASP485
4.524
VAL486
4.661
Residue
Distance (Å)
ARG489
2.851
THR513
4.264
GLY514
3.049
TRP515
4.057
ARG516
3.255
PRO517
3.408
GLY518
2.442
SER519
2.948
GLY520
3.096
PHE521
3.207
THR522
3.843
References  Top
REF 1 Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis. Nat Chem Biol. 2012 Oct;8(10):839-47.
REF 2 Structural insight into mechanisms for dynamic regulation of PKM2. Protein Cell. 2015 Apr;6(4):275-287.
REF 3 Pyruvate kinase M2 is a phosphotyrosine-binding protein. Nature. 2008 Mar 13;452(7184):181-6.
REF 4 Serine is a natural ligand and allosteric activator of pyruvate kinase M2. Nature. 2012 Nov 15;491(7424):458-462.
REF 5 Fragment-based drug discovery using cryo-EM. Drug Discov Today. 2020 Mar;25(3):485-490.
REF 6 Activator-Bound Structures of Human Pyruvate Kinase M2
REF 7 Activator-Bound Structures of Human Pyruvate Kinase M2
REF 8 Activator-Bound Structures of Human Pyruvate Kinase M2
REF 9 Discovery and structure-guided fragment-linking of 4-(2,3-dichlorobenzoyl)-1-methyl-pyrrole-2-carboxamide as a pyruvate kinase M2 activator. Bioorg Med Chem. 2017 Jul 1;25(13):3540-3546.
REF 10 Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation. J Biol Chem. 2020 Dec 18;295(51):17425-17440.
REF 11 Identification of residues involved in allosteric signal transmission from amino acid binding site of pyruvate kinase muscle isoform 2. PLoS One. 2023 Mar 10;18(3):e0282508.
REF 12 Biochemical and structural insights into how amino acids regulate pyruvate kinase muscle isoform 2. J Biol Chem. 2020 Apr 17;295(16):5390-5403.
REF 13 Mechanistic and Structural Insights into Cysteine-Mediated Inhibition of Pyruvate Kinase Muscle Isoform 2. Biochemistry. 2019 Sep 3;58(35):3669-3682.
REF 14 M2 pyruvate kinase provides a mechanism for nutrient sensing and regulation of cell proliferation. Proc Natl Acad Sci U S A. 2013 Apr 9;110(15):5881-6.
REF 15 Mutations in the PKM2 exon-10 region are associated with reduced allostery and increased nuclear translocation. Commun Biol. 2019 Mar 15;2:105.
REF 16 Human Pyruvate Kinase M2 Mutant C424A
REF 17 Allosetric regulation of M2 pyruvate kinase.
REF 18 Discovery of 2-((1H-benzo[d]imidazol-1-yl)methyl)-4H-pyrido[1,2-a]pyrimidin-4-ones as novel PKM2 activators. Bioorg Med Chem Lett. 2013 Jun 1;23(11):3358-63.
REF 19 Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis. Biochemistry. 2005 Jul 12;44(27):9417-29.

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