eF-site ID 12gs-AB
PDB Code 12gs
Chain A, B

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Title GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE
Classification TRANSFERASE/TRANSFERASE INHIBITOR
Compound GLUTATHIONE S-TRANSFERASE
Source Homo sapiens (Human) (GTP_HUMAN)
Sequence A:  PYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEG
SLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGK
DQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKA
LPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLI
HEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNL
PINGNGKQ
B:  PYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEG
SLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGK
DQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKA
LPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLI
HEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNL
PINGNGKQ
Description


Functional site
1) chain A
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
2) chain A
residue 8
type
sequence F
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
3) chain A
residue 10
type
sequence V
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
4) chain A
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
5) chain A
residue 38
type
sequence W
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
6) chain A
residue 44
type
sequence K
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
7) chain A
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
8) chain A
residue 52
type
sequence L
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
9) chain A
residue 53
type
sequence P
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
10) chain A
residue 64
type
sequence Q
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
11) chain A
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
12) chain A
residue 108
type
sequence Y
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
13) chain B
residue 98
type
sequence D
description BINDING SITE FOR RESIDUE 0HH A 210
source : AC1
14) chain A
residue 98
type
sequence D
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
15) chain B
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
16) chain B
residue 8
type
sequence F
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
17) chain B
residue 10
type
sequence V
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
18) chain B
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
19) chain B
residue 38
type
sequence W
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
20) chain B
residue 44
type
sequence K
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
21) chain B
residue 50
type
sequence G
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
22) chain B
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
23) chain B
residue 52
type
sequence L
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
24) chain B
residue 53
type
sequence P
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
25) chain B
residue 64
type
sequence Q
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
26) chain B
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
27) chain B
residue 108
type
sequence Y
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
28) chain B
residue 205
type
sequence G
description BINDING SITE FOR RESIDUE 0HH B 210
source : AC2
29) chain A
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE MES A 211
source : AC3
30) chain A
residue 28
type
sequence W
description BINDING SITE FOR RESIDUE MES A 211
source : AC3
31) chain A
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE MES A 211
source : AC3
32) chain A
residue 197
type
sequence E
description BINDING SITE FOR RESIDUE MES A 211
source : AC3
33) chain B
residue 171
type
sequence D
description BINDING SITE FOR RESIDUE MES A 211
source : AC3
34) chain A
residue 171
type
sequence D
description BINDING SITE FOR RESIDUE MES B 211
source : AC4
35) chain B
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE MES B 211
source : AC4
36) chain B
residue 28
type
sequence W
description BINDING SITE FOR RESIDUE MES B 211
source : AC4
37) chain B
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE MES B 211
source : AC4
38) chain B
residue 197
type
sequence E
description BINDING SITE FOR RESIDUE MES B 211
source : AC4
39) chain A
residue 4
type MOD_RES
sequence T
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
40) chain A
residue 199
type MOD_RES
sequence V
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
41) chain B
residue 4
type MOD_RES
sequence T
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
42) chain B
residue 199
type MOD_RES
sequence V
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
43) chain A
residue 62
type MOD_RES
sequence L
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3
44) chain B
residue 62
type MOD_RES
sequence L
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3
45) chain A
residue 103
type MOD_RES
sequence Y
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
46) chain A
residue 116
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
47) chain B
residue 103
type MOD_RES
sequence Y
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
48) chain B
residue 116
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
49) chain A
residue 8
type BINDING
sequence F
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 45
type BINDING
sequence A
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 52
type BINDING
sequence L
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 65
type BINDING
sequence S
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 14
type BINDING
sequence C
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
54) chain A
residue 39
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
55) chain A
residue 45
type BINDING
sequence A
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
56) chain A
residue 52
type BINDING
sequence L
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
57) chain A
residue 65
type BINDING
sequence S
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
58) chain B
residue 8
type BINDING
sequence F
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
59) chain B
residue 14
type BINDING
sequence C
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
60) chain B
residue 39
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
61) chain A
residue 128
type MOD_RES
sequence P
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5
62) chain B
residue 128
type MOD_RES
sequence P
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5

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