eF-site ID 1pgt-AB
PDB Code 1pgt
Chain A, B

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Title CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH S-HEXYLGLUTATHIONE
Classification TRANSFERASE
Compound GLUTATHIONE S-TRANSFERASE
Source Homo sapiens (Human) (GSTP1_HUMAN)
Sequence A:  MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQ
EGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLY
GKDQQEAALVDMVNDGVEDLRCKYVSLIYTNYEAGKDDYV
KALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLL
LIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYV
NLPINGNGKQ
B:  PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQE
GSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYG
KDQQEAALVDMVNDGVEDLRCKYVSLIYTNYEAGKDDYVK
ALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLL
IHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVN
LPINGNGKQ
Description


Functional site
1) chain A
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
2) chain A
residue 8
type
sequence F
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
3) chain A
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
4) chain A
residue 35
type
sequence V
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
5) chain A
residue 38
type
sequence W
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
6) chain A
residue 44
type
sequence K
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
7) chain A
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
8) chain A
residue 52
type
sequence L
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
9) chain A
residue 53
type
sequence P
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
10) chain A
residue 64
type
sequence Q
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
11) chain A
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
12) chain A
residue 108
type
sequence Y
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
13) chain B
residue 98
type
sequence D
description BINDING SITE FOR RESIDUE GTX A 210
source : AC1
14) chain A
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE EPE A 211
source : AC2
15) chain A
residue 28
type
sequence W
description BINDING SITE FOR RESIDUE EPE A 211
source : AC2
16) chain A
residue 29
type
sequence K
description BINDING SITE FOR RESIDUE EPE A 211
source : AC2
17) chain A
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE EPE A 211
source : AC2
18) chain A
residue 197
type
sequence E
description BINDING SITE FOR RESIDUE EPE A 211
source : AC2
19) chain B
residue 171
type
sequence D
description BINDING SITE FOR RESIDUE EPE A 211
source : AC2
20) chain A
residue 98
type
sequence D
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
21) chain B
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
22) chain B
residue 8
type
sequence F
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
23) chain B
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
24) chain B
residue 35
type
sequence V
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
25) chain B
residue 38
type
sequence W
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
26) chain B
residue 44
type
sequence K
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
27) chain B
residue 50
type
sequence G
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
28) chain B
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
29) chain B
residue 52
type
sequence L
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
30) chain B
residue 53
type
sequence P
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
31) chain B
residue 64
type
sequence Q
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
32) chain B
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
33) chain B
residue 108
type
sequence Y
description BINDING SITE FOR RESIDUE GTX B 210
source : AC3
34) chain A
residue 171
type
sequence D
description BINDING SITE FOR RESIDUE EPE B 211
source : AC4
35) chain B
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE EPE B 211
source : AC4
36) chain B
residue 28
type
sequence W
description BINDING SITE FOR RESIDUE EPE B 211
source : AC4
37) chain B
residue 29
type
sequence K
description BINDING SITE FOR RESIDUE EPE B 211
source : AC4
38) chain B
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE EPE B 211
source : AC4
39) chain B
residue 197
type
sequence E
description BINDING SITE FOR RESIDUE EPE B 211
source : AC4
40) chain A
residue 7
type catalytic
sequence Y
description 993
source MCSA : MCSA1
41) chain A
residue 7
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518
source Swiss-Prot : SWS_FT_FI1
42) chain B
residue 44
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518
source Swiss-Prot : SWS_FT_FI1
43) chain B
residue 51
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518
source Swiss-Prot : SWS_FT_FI1
44) chain B
residue 64
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518
source Swiss-Prot : SWS_FT_FI1
45) chain A
residue 13
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518
source Swiss-Prot : SWS_FT_FI1
46) chain A
residue 38
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518
source Swiss-Prot : SWS_FT_FI1
47) chain A
residue 44
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518
source Swiss-Prot : SWS_FT_FI1
48) chain A
residue 51
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518
source Swiss-Prot : SWS_FT_FI1
49) chain A
residue 64
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518
source Swiss-Prot : SWS_FT_FI1
50) chain B
residue 7
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518
source Swiss-Prot : SWS_FT_FI1
51) chain B
residue 13
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518
source Swiss-Prot : SWS_FT_FI1
52) chain B
residue 38
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518
source Swiss-Prot : SWS_FT_FI1
53) chain A
residue 3
type MOD_RES
sequence Y
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
54) chain A
residue 198
type MOD_RES
sequence Y
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
55) chain B
residue 3
type MOD_RES
sequence Y
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
56) chain B
residue 198
type MOD_RES
sequence Y
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
57) chain A
residue 61
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3
58) chain B
residue 61
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3
59) chain A
residue 102
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
60) chain A
residue 115
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
61) chain B
residue 102
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
62) chain B
residue 115
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
63) chain A
residue 127
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5
64) chain B
residue 127
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5

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