eF-site ID 1gsf-ABCD
PDB Code 1gsf
Chain A, B, C, D

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Title GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH ETHACRYNIC ACID
Classification TRANSFERASE (GLUTATHIONE)
Compound GLUTATHIONE TRANSFERASE A1-1
Source null (GSTA1_HUMAN)
Sequence A:  AEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDL
DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL
YGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKL
ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV
ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG
SPRKPPMDEKSLEEARKIFRF
B:  AEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDL
DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL
YGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKL
ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV
ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG
SPRKPPMDEKSLEEARKIFRF
C:  AEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDL
DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL
YGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKL
ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV
ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG
SPRKPPMDEKSLEEARKIFRF
D:  AEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDL
DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL
YGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKL
ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV
ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG
SPRKPPMDEKSLEEARKIFRF
Description


Functional site
1) chain A
residue 9
type
sequence Y
description BINDING SITE FOR RESIDUE EAA A 223
source : AC1
2) chain A
residue 10
type
sequence F
description BINDING SITE FOR RESIDUE EAA A 223
source : AC1
3) chain A
residue 14
type
sequence G
description BINDING SITE FOR RESIDUE EAA A 223
source : AC1
4) chain A
residue 15
type
sequence R
description BINDING SITE FOR RESIDUE EAA A 223
source : AC1
5) chain A
residue 55
type
sequence V
description BINDING SITE FOR RESIDUE EAA A 223
source : AC1
6) chain A
residue 107
type
sequence L
description BINDING SITE FOR RESIDUE EAA A 223
source : AC1
7) chain A
residue 111
type
sequence V
description BINDING SITE FOR RESIDUE EAA A 223
source : AC1
8) chain A
residue 208
type
sequence M
description BINDING SITE FOR RESIDUE EAA A 223
source : AC1
9) chain A
residue 220
type
sequence F
description BINDING SITE FOR RESIDUE EAA A 223
source : AC1
10) chain B
residue 9
type
sequence Y
description BINDING SITE FOR RESIDUE EAA B 223
source : AC2
11) chain B
residue 10
type
sequence F
description BINDING SITE FOR RESIDUE EAA B 223
source : AC2
12) chain B
residue 14
type
sequence G
description BINDING SITE FOR RESIDUE EAA B 223
source : AC2
13) chain B
residue 15
type
sequence R
description BINDING SITE FOR RESIDUE EAA B 223
source : AC2
14) chain B
residue 55
type
sequence V
description BINDING SITE FOR RESIDUE EAA B 223
source : AC2
15) chain B
residue 107
type
sequence L
description BINDING SITE FOR RESIDUE EAA B 223
source : AC2
16) chain B
residue 111
type
sequence V
description BINDING SITE FOR RESIDUE EAA B 223
source : AC2
17) chain B
residue 208
type
sequence M
description BINDING SITE FOR RESIDUE EAA B 223
source : AC2
18) chain B
residue 220
type
sequence F
description BINDING SITE FOR RESIDUE EAA B 223
source : AC2
19) chain C
residue 9
type
sequence Y
description BINDING SITE FOR RESIDUE EAA C 223
source : AC3
20) chain C
residue 10
type
sequence F
description BINDING SITE FOR RESIDUE EAA C 223
source : AC3
21) chain C
residue 14
type
sequence G
description BINDING SITE FOR RESIDUE EAA C 223
source : AC3
22) chain C
residue 15
type
sequence R
description BINDING SITE FOR RESIDUE EAA C 223
source : AC3
23) chain C
residue 55
type
sequence V
description BINDING SITE FOR RESIDUE EAA C 223
source : AC3
24) chain C
residue 107
type
sequence L
description BINDING SITE FOR RESIDUE EAA C 223
source : AC3
25) chain C
residue 111
type
sequence V
description BINDING SITE FOR RESIDUE EAA C 223
source : AC3
26) chain C
residue 208
type
sequence M
description BINDING SITE FOR RESIDUE EAA C 223
source : AC3
27) chain C
residue 220
type
sequence F
description BINDING SITE FOR RESIDUE EAA C 223
source : AC3
28) chain D
residue 9
type
sequence Y
description BINDING SITE FOR RESIDUE EAA D 223
source : AC4
29) chain D
residue 10
type
sequence F
description BINDING SITE FOR RESIDUE EAA D 223
source : AC4
30) chain D
residue 14
type
sequence G
description BINDING SITE FOR RESIDUE EAA D 223
source : AC4
31) chain D
residue 15
type
sequence R
description BINDING SITE FOR RESIDUE EAA D 223
source : AC4
32) chain D
residue 55
type
sequence V
description BINDING SITE FOR RESIDUE EAA D 223
source : AC4
33) chain D
residue 107
type
sequence L
description BINDING SITE FOR RESIDUE EAA D 223
source : AC4
34) chain D
residue 111
type
sequence V
description BINDING SITE FOR RESIDUE EAA D 223
source : AC4
35) chain D
residue 208
type
sequence M
description BINDING SITE FOR RESIDUE EAA D 223
source : AC4
36) chain D
residue 220
type
sequence F
description BINDING SITE FOR RESIDUE EAA D 223
source : AC4
37) chain A
residue 5
type MOD_RES
sequence P
description N6-succinyllysine => ECO:0000250|UniProtKB:P30115
source Swiss-Prot : SWS_FT_FI4
38) chain B
residue 5
type MOD_RES
sequence P
description N6-succinyllysine => ECO:0000250|UniProtKB:P30115
source Swiss-Prot : SWS_FT_FI4
39) chain C
residue 5
type MOD_RES
sequence P
description N6-succinyllysine => ECO:0000250|UniProtKB:P30115
source Swiss-Prot : SWS_FT_FI4
40) chain D
residue 5
type MOD_RES
sequence P
description N6-succinyllysine => ECO:0000250|UniProtKB:P30115
source Swiss-Prot : SWS_FT_FI4
41) chain A
residue 10
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
42) chain A
residue 46
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
43) chain A
residue 55
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
44) chain A
residue 68
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
45) chain B
residue 10
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
46) chain B
residue 46
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
47) chain B
residue 55
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
48) chain B
residue 68
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
49) chain C
residue 46
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
50) chain C
residue 55
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
51) chain C
residue 68
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
52) chain D
residue 10
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
53) chain D
residue 46
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
54) chain D
residue 55
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
55) chain D
residue 68
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
56) chain C
residue 10
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
57) chain C
residue 2
type MOD_RES
sequence A
description N-acetylmethionine => ECO:0000250|UniProtKB:P80894
source Swiss-Prot : SWS_FT_FI2
58) chain D
residue 2
type MOD_RES
sequence A
description N-acetylmethionine => ECO:0000250|UniProtKB:P80894
source Swiss-Prot : SWS_FT_FI2
59) chain A
residue 2
type MOD_RES
sequence A
description N-acetylmethionine => ECO:0000250|UniProtKB:P80894
source Swiss-Prot : SWS_FT_FI2
60) chain B
residue 2
type MOD_RES
sequence A
description N-acetylmethionine => ECO:0000250|UniProtKB:P80894
source Swiss-Prot : SWS_FT_FI2
61) 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
62) 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
63) chain C
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
64) chain D
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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