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

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Title GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM
Classification TRANSFERASE (GLUTATHIONE)
Compound GLUTATHIONE TRANSFERASE A1-1
Source Homo sapiens (Human) (GSTA1_HUMAN)
Sequence A:  AEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDL
DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL
YGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKL
ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV
ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG
SPRKPPMD
B:  AEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDL
DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL
YGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKL
ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV
ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG
SPRKPPMD
C:  AEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDL
DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL
YGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKL
ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV
ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG
SPRKPPMD
D:  AEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDL
DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL
YGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKL
ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV
ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG
SPRKPPMD
Description


Functional site
1) chain A
residue 10
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
2) chain C
residue 46
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
3) chain C
residue 55
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
4) chain C
residue 68
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
5) chain D
residue 10
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
6) chain D
residue 46
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
7) chain D
residue 55
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
8) chain D
residue 68
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
9) chain A
residue 46
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
10) chain A
residue 55
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
11) chain A
residue 68
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
12) chain B
residue 10
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
13) chain B
residue 46
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
14) chain B
residue 55
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
15) chain B
residue 68
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
16) chain C
residue 10
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
source Swiss-Prot : SWS_FT_FI1
17) chain A
residue 2
type MOD_RES
sequence A
description N-acetylmethionine => ECO:0000250|UniProtKB:P80894
source Swiss-Prot : SWS_FT_FI2
18) chain B
residue 2
type MOD_RES
sequence A
description N-acetylmethionine => ECO:0000250|UniProtKB:P80894
source Swiss-Prot : SWS_FT_FI2
19) chain C
residue 2
type MOD_RES
sequence A
description N-acetylmethionine => ECO:0000250|UniProtKB:P80894
source Swiss-Prot : SWS_FT_FI2
20) chain D
residue 2
type MOD_RES
sequence A
description N-acetylmethionine => ECO:0000250|UniProtKB:P80894
source Swiss-Prot : SWS_FT_FI2
21) 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
22) 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
23) 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
24) 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
25) chain A
residue 5
type MOD_RES
sequence P
description N6-succinyllysine => ECO:0000250|UniProtKB:P30115
source Swiss-Prot : SWS_FT_FI4
26) chain B
residue 5
type MOD_RES
sequence P
description N6-succinyllysine => ECO:0000250|UniProtKB:P30115
source Swiss-Prot : SWS_FT_FI4
27) chain C
residue 5
type MOD_RES
sequence P
description N6-succinyllysine => ECO:0000250|UniProtKB:P30115
source Swiss-Prot : SWS_FT_FI4
28) chain D
residue 5
type MOD_RES
sequence P
description N6-succinyllysine => ECO:0000250|UniProtKB:P30115
source Swiss-Prot : SWS_FT_FI4

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