eF-site ID 18gs-A
PDB Code 18gs
Chain A

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Title GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENE
Classification TRANSFERASE
Compound GLUTATHIONE S-TRANSFERASE
Source Homo sapiens (Human) (GSTP1_HUMAN)
Sequence A:  PYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEG
SLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGK
DQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKA
LPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLI
HEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNL
PINGNGKQ
Description


Functional site

1) chain A
residue 8
type
sequence F
description BINDING SITE FOR RESIDUE GDN A 210
source : AC1

2) chain A
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE GDN A 210
source : AC1

3) chain A
residue 38
type
sequence W
description BINDING SITE FOR RESIDUE GDN A 210
source : AC1

4) chain A
residue 44
type
sequence K
description BINDING SITE FOR RESIDUE GDN A 210
source : AC1

5) chain A
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE GDN A 210
source : AC1

6) chain A
residue 52
type
sequence L
description BINDING SITE FOR RESIDUE GDN A 210
source : AC1

7) chain A
residue 53
type
sequence P
description BINDING SITE FOR RESIDUE GDN A 210
source : AC1

8) chain A
residue 64
type
sequence Q
description BINDING SITE FOR RESIDUE GDN A 210
source : AC1

9) chain A
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE GDN A 210
source : AC1

10) chain A
residue 104
type
sequence I
description BINDING SITE FOR RESIDUE GDN A 210
source : AC1

11) chain A
residue 108
type
sequence Y
description BINDING SITE FOR RESIDUE GDN A 210
source : AC1

12) chain A
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE MES A 211
source : AC2

13) chain A
residue 28
type
sequence W
description BINDING SITE FOR RESIDUE MES A 211
source : AC2

14) chain A
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE MES A 211
source : AC2

15) chain A
residue 197
type
sequence E
description BINDING SITE FOR RESIDUE MES A 211
source : AC2

16) chain A
residue 98
type
sequence D
description BINDING SITE FOR RESIDUE GDN B 210
source : AC3

17) chain A
residue 4
type MOD_RES
sequence T
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2

18) chain A
residue 199
type MOD_RES
sequence V
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2

19) chain A
residue 128
type MOD_RES
sequence P
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5

20) 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

21) 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

22) 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

23) 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

24) 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

25) 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

26) chain A
residue 62
type MOD_RES
sequence L
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

27) chain A
residue 103
type MOD_RES
sequence Y
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4

28) chain A
residue 116
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4


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