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

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Title GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH AN ETHACRYNIC ACID GLUTATHIONE CONJUGATE (MUTANT R15K)
Classification TRANSFERASE (GLUTATHIONE)
Compound GLUTATHIONE TRANSFERASE
Source Homo sapiens (Human) (GTA1_HUMAN)
Sequence A:  AEKPKLHYFNARGKMESTRWLLAAAGVEFEEKFIKSAEDL
DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL
YGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKL
ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV
ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG
SPRKPPMDEKSLEEARKIFRF
B:  AEKPKLHYFNARGKMESTRWLLAAAGVEFEEKFIKSAEDL
DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL
YGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKL
ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV
ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG
SPRKPPMDEKSLEEARKIFRF
Description


Functional site

1) chain A
residue 9
type
sequence Y
description BINDING SITE FOR RESIDUE GSH A 223
source : AC1

2) chain A
residue 45
type
sequence R
description BINDING SITE FOR RESIDUE GSH A 223
source : AC1

3) chain A
residue 54
type
sequence Q
description BINDING SITE FOR RESIDUE GSH A 223
source : AC1

4) chain A
residue 55
type
sequence V
description BINDING SITE FOR RESIDUE GSH A 223
source : AC1

5) chain A
residue 56
type
sequence P
description BINDING SITE FOR RESIDUE GSH A 223
source : AC1

6) chain A
residue 67
type
sequence Q
description BINDING SITE FOR RESIDUE GSH A 223
source : AC1

7) chain A
residue 68
type
sequence T
description BINDING SITE FOR RESIDUE GSH A 223
source : AC1

8) chain B
residue 101
type
sequence D
description BINDING SITE FOR RESIDUE GSH A 223
source : AC1

9) chain B
residue 131
type
sequence R
description BINDING SITE FOR RESIDUE GSH A 223
source : AC1

10) chain A
residue 9
type
sequence Y
description BINDING SITE FOR RESIDUE EAA A 224
source : AC2

11) chain A
residue 10
type
sequence F
description BINDING SITE FOR RESIDUE EAA A 224
source : AC2

12) chain A
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE EAA A 224
source : AC2

13) chain A
residue 14
type
sequence G
description BINDING SITE FOR RESIDUE EAA A 224
source : AC2

14) chain A
residue 15
type
sequence K
description BINDING SITE FOR RESIDUE EAA A 224
source : AC2

15) chain A
residue 107
type
sequence L
description BINDING SITE FOR RESIDUE EAA A 224
source : AC2

16) chain A
residue 108
type
sequence L
description BINDING SITE FOR RESIDUE EAA A 224
source : AC2

17) chain A
residue 111
type
sequence V
description BINDING SITE FOR RESIDUE EAA A 224
source : AC2

18) chain A
residue 208
type
sequence M
description BINDING SITE FOR RESIDUE EAA A 224
source : AC2

19) chain A
residue 216
type
sequence A
description BINDING SITE FOR RESIDUE EAA A 224
source : AC2

20) chain A
residue 220
type
sequence F
description BINDING SITE FOR RESIDUE EAA A 224
source : AC2

21) chain A
residue 222
type
sequence F
description BINDING SITE FOR RESIDUE EAA A 224
source : AC2

22) chain A
residue 18
type
sequence S
description BINDING SITE FOR RESIDUE BME A 225
source : AC3

23) chain A
residue 96
type
sequence I
description BINDING SITE FOR RESIDUE BME A 225
source : AC3

24) chain A
residue 69
type
sequence R
description BINDING SITE FOR RESIDUE BME A 226
source : AC4

25) chain A
residue 72
type
sequence L
description BINDING SITE FOR RESIDUE BME A 226
source : AC4

26) chain A
residue 96
type
sequence I
description BINDING SITE FOR RESIDUE BME A 226
source : AC4

27) chain A
residue 97
type
sequence E
description BINDING SITE FOR RESIDUE BME A 226
source : AC4

28) chain A
residue 159
type
sequence H
description BINDING SITE FOR RESIDUE BME A 226
source : AC4

29) chain A
residue 101
type
sequence D
description BINDING SITE FOR RESIDUE GSH B 223
source : AC5

30) chain A
residue 131
type
sequence R
description BINDING SITE FOR RESIDUE GSH B 223
source : AC5

31) chain B
residue 9
type
sequence Y
description BINDING SITE FOR RESIDUE GSH B 223
source : AC5

32) chain B
residue 45
type
sequence R
description BINDING SITE FOR RESIDUE GSH B 223
source : AC5

33) chain B
residue 54
type
sequence Q
description BINDING SITE FOR RESIDUE GSH B 223
source : AC5

34) chain B
residue 55
type
sequence V
description BINDING SITE FOR RESIDUE GSH B 223
source : AC5

35) chain B
residue 56
type
sequence P
description BINDING SITE FOR RESIDUE GSH B 223
source : AC5

36) chain B
residue 67
type
sequence Q
description BINDING SITE FOR RESIDUE GSH B 223
source : AC5

37) chain B
residue 68
type
sequence T
description BINDING SITE FOR RESIDUE GSH B 223
source : AC5

38) chain B
residue 9
type
sequence Y
description BINDING SITE FOR RESIDUE EAA B 224
source : AC6

39) chain B
residue 10
type
sequence F
description BINDING SITE FOR RESIDUE EAA B 224
source : AC6

40) chain B
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE EAA B 224
source : AC6

41) chain B
residue 14
type
sequence G
description BINDING SITE FOR RESIDUE EAA B 224
source : AC6

42) chain B
residue 15
type
sequence K
description BINDING SITE FOR RESIDUE EAA B 224
source : AC6

43) chain B
residue 107
type
sequence L
description BINDING SITE FOR RESIDUE EAA B 224
source : AC6

44) chain B
residue 108
type
sequence L
description BINDING SITE FOR RESIDUE EAA B 224
source : AC6

45) chain B
residue 110
type
sequence P
description BINDING SITE FOR RESIDUE EAA B 224
source : AC6

46) chain B
residue 111
type
sequence V
description BINDING SITE FOR RESIDUE EAA B 224
source : AC6

47) chain B
residue 208
type
sequence M
description BINDING SITE FOR RESIDUE EAA B 224
source : AC6

48) chain B
residue 216
type
sequence A
description BINDING SITE FOR RESIDUE EAA B 224
source : AC6

49) chain B
residue 220
type
sequence F
description BINDING SITE FOR RESIDUE EAA B 224
source : AC6

50) chain B
residue 18
type
sequence S
description BINDING SITE FOR RESIDUE BME B 225
source : AC7

51) chain B
residue 96
type
sequence I
description BINDING SITE FOR RESIDUE BME B 225
source : AC7

52) chain B
residue 69
type
sequence R
description BINDING SITE FOR RESIDUE BME B 226
source : AC8

53) chain B
residue 96
type
sequence I
description BINDING SITE FOR RESIDUE BME B 226
source : AC8

54) chain B
residue 97
type
sequence E
description BINDING SITE FOR RESIDUE BME B 226
source : AC8

55) chain B
residue 159
type
sequence H
description BINDING SITE FOR RESIDUE BME B 226
source : AC8

56) chain A
residue 10
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1

57) chain A
residue 46
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1

58) chain A
residue 55
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1

59) chain A
residue 68
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1

60) chain B
residue 10
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1

61) chain B
residue 46
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1

62) chain B
residue 55
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1

63) chain B
residue 68
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1

64) chain A
residue 5
type MOD_RES
sequence P
description N6-succinyllysine => ECO:0000250|UniProtKB:P30115
source Swiss-Prot : SWS_FT_FI4

65) chain B
residue 5
type MOD_RES
sequence P
description N6-succinyllysine => ECO:0000250|UniProtKB:P30115
source Swiss-Prot : SWS_FT_FI4

66) chain A
residue 2
type MOD_RES
sequence A
description N-acetylmethionine => ECO:0000250|UniProtKB:P80894
source Swiss-Prot : SWS_FT_FI2

67) chain B
residue 2
type MOD_RES
sequence A
description N-acetylmethionine => ECO:0000250|UniProtKB:P80894
source Swiss-Prot : SWS_FT_FI2

68) chain A
residue 3
type MOD_RES
sequence E
description N-acetylalanine; in Glutathione S-transferase A1, N-terminally processed => ECO:0000250|UniProtKB:P30115
source Swiss-Prot : SWS_FT_FI3

69) chain B
residue 3
type MOD_RES
sequence E
description N-acetylalanine; in Glutathione S-transferase A1, N-terminally processed => ECO:0000250|UniProtKB:P30115
source Swiss-Prot : SWS_FT_FI3


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