eF-site ID 5x1w-A
PDB Code 5x1w
Chain A

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Title PKM2 in complex with compound 5
Classification TRANSFERASE
Compound Pyruvate kinase PKM
Source (KPYM_HUMAN)
Sequence A:  QTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGP
ASRSVETLKEMIKSGMNVARLNFSHGTHEYHAETIKNVRT
ATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVE
LKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSK
IYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPG
AAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHE
VRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVA
RGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLES
MIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLE
AVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATA
VGAVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAV
TRNPQTARQAHLYRGIFPVLCKDPVQEAWAEDVDLRVNFA
MNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
Description


Functional site

1) chain A
residue 265-277
type prosite
sequence IKIISKIENHEGV
description PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV
source prosite : PS00110

2) chain A
residue 70
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:23064226
source Swiss-Prot : SWS_FT_FI1

3) chain A
residue 106
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:23064226
source Swiss-Prot : SWS_FT_FI1

4) chain A
residue 464
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:23064226
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 41
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI10

6) chain A
residue 62
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI11

7) chain A
residue 89
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI11

8) chain A
residue 66
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI12

9) chain A
residue 498
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI12

10) chain A
residue 97
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P11980
source Swiss-Prot : SWS_FT_FI13

11) chain A
residue 100
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P11980
source Swiss-Prot : SWS_FT_FI13

12) chain A
residue 105
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI14

13) chain A
residue 127
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI15

14) chain A
residue 148
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI16

15) chain A
residue 166
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI17

16) chain A
residue 322
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI17

17) chain A
residue 175
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI18

18) chain A
residue 195
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI19

19) chain A
residue 73
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P30613
source Swiss-Prot : SWS_FT_FI2

20) chain A
residue 270
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P30613
source Swiss-Prot : SWS_FT_FI2

21) chain A
residue 295
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P30613
source Swiss-Prot : SWS_FT_FI2

22) chain A
residue 296
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P30613
source Swiss-Prot : SWS_FT_FI2

23) chain A
residue 328
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P30613
source Swiss-Prot : SWS_FT_FI2

24) chain A
residue 266
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI20

25) chain A
residue 270
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI21

26) chain A
residue 305
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:21700219
source Swiss-Prot : SWS_FT_FI22

27) chain A
residue 403
type MOD_RES
sequence P
description 4-hydroxyproline => ECO:0000269|PubMed:21620138
source Swiss-Prot : SWS_FT_FI23

28) chain A
residue 408
type MOD_RES
sequence P
description 4-hydroxyproline => ECO:0000269|PubMed:21620138
source Swiss-Prot : SWS_FT_FI23

29) chain A
residue 423
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000269|PubMed:30487609
source Swiss-Prot : SWS_FT_FI24

30) chain A
residue 424
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000269|PubMed:30487609
source Swiss-Prot : SWS_FT_FI24

31) chain A
residue 433
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI25

32) chain A
residue 475
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI26

33) chain A
residue 115
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI27

34) chain A
residue 266
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI28

35) chain A
residue 270
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI28

36) chain A
residue 166
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211
source Swiss-Prot : SWS_FT_FI29

37) chain A
residue 75
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3

38) chain A
residue 77
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3

39) chain A
residue 113
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3

40) chain A
residue 114
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3

41) chain A
residue 120
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3

42) chain A
residue 207
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3

43) chain A
residue 272
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3

44) chain A
residue 432
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI4

45) chain A
residue 482
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI4

46) chain A
residue 489
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI4

47) chain A
residue 516
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI4

48) chain A
residue 270
type SITE
sequence K
description Transition state stabilizer => ECO:0000250|UniProtKB:P00549
source Swiss-Prot : SWS_FT_FI5

49) chain A
residue 433
type SITE
sequence K
description Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445
source Swiss-Prot : SWS_FT_FI6

50) chain A
residue 37
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9


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