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

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Title Crystal Structure of the Glutathione Transferase Pi in Complex with Dinitrosyl-diglutathionyl Iron Complex
Classification TRANSFERASE
Compound Glutathione S-transferase P
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 7
type
sequence Y
description BINDING SITE FOR RESIDUE FE A 1222
source : AC1
2) chain B
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE FE B 2222
source : AC2
3) chain A
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE MES A 1220
source : AC3
4) chain A
residue 26
type
sequence Q
description BINDING SITE FOR RESIDUE MES A 1220
source : AC3
5) chain A
residue 28
type
sequence W
description BINDING SITE FOR RESIDUE MES A 1220
source : AC3
6) chain A
residue 197
type
sequence E
description BINDING SITE FOR RESIDUE MES A 1220
source : AC3
7) chain B
residue 171
type
sequence D
description BINDING SITE FOR RESIDUE MES A 1220
source : AC3
8) chain A
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE GSH A 1221
source : AC4
9) chain A
residue 8
type
sequence F
description BINDING SITE FOR RESIDUE GSH A 1221
source : AC4
10) chain A
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE GSH A 1221
source : AC4
11) chain A
residue 38
type
sequence W
description BINDING SITE FOR RESIDUE GSH A 1221
source : AC4
12) chain A
residue 44
type
sequence K
description BINDING SITE FOR RESIDUE GSH A 1221
source : AC4
13) chain A
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE GSH A 1221
source : AC4
14) chain A
residue 52
type
sequence L
description BINDING SITE FOR RESIDUE GSH A 1221
source : AC4
15) chain A
residue 64
type
sequence Q
description BINDING SITE FOR RESIDUE GSH A 1221
source : AC4
16) chain A
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE GSH A 1221
source : AC4
17) chain B
residue 98
type
sequence D
description BINDING SITE FOR RESIDUE GSH A 1221
source : AC4
18) chain A
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE NO A 1223
source : AC5
19) chain A
residue 12
type
sequence G
description BINDING SITE FOR RESIDUE NO A 1223
source : AC5
20) chain A
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE NO A 1223
source : AC5
21) chain A
residue 104
type
sequence I
description BINDING SITE FOR RESIDUE NO A 1223
source : AC5
22) chain A
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE NO A 1224
source : AC6
23) chain A
residue 8
type
sequence F
description BINDING SITE FOR RESIDUE NO A 1224
source : AC6
24) chain A
residue 108
type
sequence Y
description BINDING SITE FOR RESIDUE NO A 1224
source : AC6
25) chain A
residue 172
type
sequence A
description BINDING SITE FOR RESIDUE MES B 2220
source : AC7
26) chain B
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE MES B 2220
source : AC7
27) chain B
residue 28
type
sequence W
description BINDING SITE FOR RESIDUE MES B 2220
source : AC7
28) chain B
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE MES B 2220
source : AC7
29) chain B
residue 192
type
sequence F
description BINDING SITE FOR RESIDUE MES B 2220
source : AC7
30) chain B
residue 197
type
sequence E
description BINDING SITE FOR RESIDUE MES B 2220
source : AC7
31) chain A
residue 98
type
sequence D
description BINDING SITE FOR RESIDUE GSH B 2221
source : AC8
32) chain B
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE GSH B 2221
source : AC8
33) chain B
residue 8
type
sequence F
description BINDING SITE FOR RESIDUE GSH B 2221
source : AC8
34) chain B
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE GSH B 2221
source : AC8
35) chain B
residue 38
type
sequence W
description BINDING SITE FOR RESIDUE GSH B 2221
source : AC8
36) chain B
residue 44
type
sequence K
description BINDING SITE FOR RESIDUE GSH B 2221
source : AC8
37) chain B
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE GSH B 2221
source : AC8
38) chain B
residue 52
type
sequence L
description BINDING SITE FOR RESIDUE GSH B 2221
source : AC8
39) chain B
residue 64
type
sequence Q
description BINDING SITE FOR RESIDUE GSH B 2221
source : AC8
40) chain B
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE GSH B 2221
source : AC8
41) chain B
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE NO B 2223
source : AC9
42) chain B
residue 12
type
sequence G
description BINDING SITE FOR RESIDUE NO B 2223
source : AC9
43) chain B
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE NO B 2223
source : AC9
44) chain B
residue 104
type
sequence I
description BINDING SITE FOR RESIDUE NO B 2223
source : AC9
45) chain B
residue 108
type
sequence Y
description BINDING SITE FOR RESIDUE NO B 2224
source : BC1
46) 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
47) 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
48) 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
49) 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
50) 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
51) 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
52) 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
53) 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
54) 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
55) 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
56) 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
57) 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
58) chain A
residue 4
type MOD_RES
sequence T
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
59) chain A
residue 199
type MOD_RES
sequence V
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
60) chain B
residue 4
type MOD_RES
sequence T
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
61) chain B
residue 199
type MOD_RES
sequence V
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2
62) chain A
residue 62
type MOD_RES
sequence L
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3
63) chain B
residue 62
type MOD_RES
sequence L
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3
64) chain A
residue 103
type MOD_RES
sequence Y
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
65) chain A
residue 116
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
66) chain B
residue 103
type MOD_RES
sequence Y
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
67) chain B
residue 116
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4
68) chain A
residue 128
type MOD_RES
sequence P
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5
69) 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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