eF-site ID 4qgc-B
PDB Code 4qgc
Chain B

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Title crystal structure of PKM2-K422R mutant
Classification TRANSFERASE
Compound Pyruvate kinase PKM
Source Homo sapiens (Human) (KPYM_HUMAN)
Sequence B:  DTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKE
MIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPI
LYRPVAVALDTKGPEIRTGLIKGAEVELKKGATLKITLDN
AYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVK
QKGADFLVTEVENGGSLGSKKGVNLPDLPAVSEKDIQDLK
FGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISK
IENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQ
KMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVAN
AVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAIY
HLQLFEELRRLAPSDPTEATAVGAVEASFRCCSGAIIVLT
KSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPV
LCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVL
TGWRPGSGFTNTMRVVPVP
Description


Functional site
1) chain B
residue 75
type
sequence N
description BINDING SITE FOR RESIDUE K B 1001
source : AC6
2) chain B
residue 77
type
sequence S
description BINDING SITE FOR RESIDUE K B 1001
source : AC6
3) chain B
residue 113
type
sequence D
description BINDING SITE FOR RESIDUE K B 1001
source : AC6
4) chain B
residue 114
type
sequence T
description BINDING SITE FOR RESIDUE K B 1001
source : AC6
5) chain B
residue 432
type
sequence T
description BINDING SITE FOR RESIDUE SO4 B 1002
source : AC7
6) chain B
residue 433
type
sequence K
description BINDING SITE FOR RESIDUE SO4 B 1002
source : AC7
7) chain B
residue 434
type
sequence S
description BINDING SITE FOR RESIDUE SO4 B 1002
source : AC7
8) chain B
residue 435
type
sequence G
description BINDING SITE FOR RESIDUE SO4 B 1002
source : AC7
9) chain B
residue 436
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 1002
source : AC7
10) chain B
residue 437
type
sequence S
description BINDING SITE FOR RESIDUE SO4 B 1002
source : AC7
11) chain B
residue 433
type
sequence K
description BINDING SITE FOR RESIDUE SO4 B 1003
source : AC8
12) chain B
residue 482
type
sequence W
description BINDING SITE FOR RESIDUE SO4 B 1003
source : AC8
13) chain B
residue 489
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 1003
source : AC8
14) chain B
residue 43
type
sequence R
description BINDING SITE FOR RESIDUE GOL B 1004
source : AC9
15) chain B
residue 44
type
sequence N
description BINDING SITE FOR RESIDUE GOL B 1004
source : AC9
16) chain B
residue 70
type
sequence N
description BINDING SITE FOR RESIDUE GOL B 1004
source : AC9
17) chain B
residue 464
type
sequence H
description BINDING SITE FOR RESIDUE GOL B 1004
source : AC9
18) chain B
residue 466
type
sequence Y
description BINDING SITE FOR RESIDUE GOL B 1004
source : AC9
19) chain B
residue 469
type
sequence I
description BINDING SITE FOR RESIDUE GOL B 1004
source : AC9
20) chain B
residue 471
type
sequence P
description BINDING SITE FOR RESIDUE GOL B 1004
source : AC9
21) chain B
residue 70
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:23064226
source Swiss-Prot : SWS_FT_FI1
22) chain B
residue 106
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:23064226
source Swiss-Prot : SWS_FT_FI1
23) chain B
residue 464
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:23064226
source Swiss-Prot : SWS_FT_FI1
24) chain B
residue 41
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI10
25) chain B
residue 62
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI11
26) chain B
residue 89
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI11
27) chain B
residue 305
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:21700219
source Swiss-Prot : SWS_FT_FI22
28) chain B
residue 403
type MOD_RES
sequence P
description 4-hydroxyproline => ECO:0000269|PubMed:21620138
source Swiss-Prot : SWS_FT_FI23
29) chain B
residue 408
type MOD_RES
sequence P
description 4-hydroxyproline => ECO:0000269|PubMed:21620138
source Swiss-Prot : SWS_FT_FI23
30) chain B
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_FI24
31) chain B
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_FI27
32) chain B
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_FI27
33) chain B
residue 475
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI25
34) chain B
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_FI26
35) chain B
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_FI28
36) chain B
residue 66
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI12
37) chain B
residue 498
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI12
38) chain B
residue 97
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P11980
source Swiss-Prot : SWS_FT_FI13
39) chain B
residue 100
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P11980
source Swiss-Prot : SWS_FT_FI13
40) chain B
residue 105
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI14
41) chain B
residue 148
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI16
42) chain B
residue 166
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI17
43) chain B
residue 322
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI17
44) chain B
residue 175
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI18
45) chain B
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
46) chain B
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
47) chain B
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
48) chain B
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
49) chain B
residue 270
type SITE
sequence K
description Transition state stabilizer => ECO:0000250|UniProtKB:P00549
source Swiss-Prot : SWS_FT_FI5
50) chain B
residue 195
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI19
51) chain B
residue 328
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P30613
source Swiss-Prot : SWS_FT_FI2
52) chain B
residue 73
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P30613
source Swiss-Prot : SWS_FT_FI2
53) chain B
residue 270
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P30613
source Swiss-Prot : SWS_FT_FI2
54) chain B
residue 295
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P30613
source Swiss-Prot : SWS_FT_FI2
55) chain B
residue 296
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P30613
source Swiss-Prot : SWS_FT_FI2
56) chain B
residue 266
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI20
57) chain B
residue 270
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480
source Swiss-Prot : SWS_FT_FI21
58) chain B
residue 113
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3
59) chain B
residue 114
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3
60) chain B
residue 120
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3
61) chain B
residue 207
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3
62) chain B
residue 272
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3
63) chain B
residue 75
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3
64) chain B
residue 77
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
source Swiss-Prot : SWS_FT_FI3
65) chain B
residue 433
type SITE
sequence K
description Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445
source Swiss-Prot : SWS_FT_FI6
66) chain B
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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