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

click to enlarge
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


Display surface

Download
Links