eF-site ID 19gs-AB
PDB Code 19gs
Chain A, B

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Title Glutathione s-transferase p1-1
Classification TRANSFERASE
Compound GLUTATHIONE S-TRANSFERASE
Source Homo sapiens (Human) (GSTP1_HUMAN)
Sequence A:  PYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEG
SLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGK
DQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKA
LPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLI
HEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNL
PINGNGKQ
B:  PYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEG
SLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGK
DQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKA
LPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLI
HEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNL
PINGNGKQ
Description


Functional site
1) chain A
residue 35
type
sequence V
description BINDING SITE FOR RESIDUE BSP A 210
source : AC1
2) chain A
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE BSP A 210
source : AC1
3) chain A
residue 108
type
sequence Y
description BINDING SITE FOR RESIDUE BSP A 210
source : AC1
4) chain A
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE GSH A 211
source : AC2
5) chain A
residue 8
type
sequence F
description BINDING SITE FOR RESIDUE GSH A 211
source : AC2
6) chain A
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE GSH A 211
source : AC2
7) chain A
residue 38
type
sequence W
description BINDING SITE FOR RESIDUE GSH A 211
source : AC2
8) chain A
residue 44
type
sequence K
description BINDING SITE FOR RESIDUE GSH A 211
source : AC2
9) chain A
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE GSH A 211
source : AC2
10) chain A
residue 52
type
sequence L
description BINDING SITE FOR RESIDUE GSH A 211
source : AC2
11) chain A
residue 64
type
sequence Q
description BINDING SITE FOR RESIDUE GSH A 211
source : AC2
12) chain A
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE GSH A 211
source : AC2
13) chain B
residue 98
type
sequence D
description BINDING SITE FOR RESIDUE GSH A 211
source : AC2
14) chain A
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE MES A 212
source : AC3
15) chain A
residue 28
type
sequence W
description BINDING SITE FOR RESIDUE MES A 212
source : AC3
16) chain A
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE MES A 212
source : AC3
17) chain A
residue 197
type
sequence E
description BINDING SITE FOR RESIDUE MES A 212
source : AC3
18) chain B
residue 171
type
sequence D
description BINDING SITE FOR RESIDUE MES A 212
source : AC3
19) chain B
residue 35
type
sequence V
description BINDING SITE FOR RESIDUE BSP B 210
source : AC4
20) chain B
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE BSP B 210
source : AC4
21) chain B
residue 108
type
sequence Y
description BINDING SITE FOR RESIDUE BSP B 210
source : AC4
22) chain A
residue 98
type
sequence D
description BINDING SITE FOR RESIDUE GSH B 211
source : AC5
23) chain B
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE GSH B 211
source : AC5
24) chain B
residue 8
type
sequence F
description BINDING SITE FOR RESIDUE GSH B 211
source : AC5
25) chain B
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE GSH B 211
source : AC5
26) chain B
residue 38
type
sequence W
description BINDING SITE FOR RESIDUE GSH B 211
source : AC5
27) chain B
residue 44
type
sequence K
description BINDING SITE FOR RESIDUE GSH B 211
source : AC5
28) chain B
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE GSH B 211
source : AC5
29) chain B
residue 52
type
sequence L
description BINDING SITE FOR RESIDUE GSH B 211
source : AC5
30) chain B
residue 64
type
sequence Q
description BINDING SITE FOR RESIDUE GSH B 211
source : AC5
31) chain B
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE GSH B 211
source : AC5
32) chain A
residue 171
type
sequence D
description BINDING SITE FOR RESIDUE MES B 212
source : AC6
33) chain B
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE MES B 212
source : AC6
34) chain B
residue 28
type
sequence W
description BINDING SITE FOR RESIDUE MES B 212
source : AC6
35) chain B
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE MES B 212
source : AC6
36) chain B
residue 197
type
sequence E
description BINDING SITE FOR RESIDUE MES B 212
source : AC6
37) chain A
residue 128
type MOD_RES
sequence P
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5
38) chain B
residue 128
type MOD_RES
sequence P
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5
39) 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
40) 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
41) 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
42) 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
43) 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
44) 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
45) 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
46) 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
47) 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
48) 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
49) 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
50) 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
51) chain A
residue 4
type MOD_RES
sequence T
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
52) chain A
residue 199
type MOD_RES
sequence V
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
53) chain B
residue 4
type MOD_RES
sequence T
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
54) chain B
residue 199
type MOD_RES
sequence V
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
55) chain A
residue 62
type MOD_RES
sequence L
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3
56) chain B
residue 62
type MOD_RES
sequence L
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3
57) chain A
residue 103
type MOD_RES
sequence Y
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
58) chain A
residue 116
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
59) chain B
residue 103
type MOD_RES
sequence Y
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
60) chain B
residue 116
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4

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