eF-site ID 3pgt-A
PDB Code 3pgt
Chain A

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Title CRYSTAL STRUCTURE OF HGSTP1-1[I104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE
Classification TRANSFERASE
Compound PROTEIN (GLUTATHIONE S-TRANSFERASE)
Source (GSTP1_HUMAN)
Sequence A:  MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQ
EGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLY
GKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYV
KALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLL
LIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYV
NLPINGNGKQ
Description


Functional site

1) chain A
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE SO4 A 210
source : AC2

2) chain A
residue 105
type
sequence S
description BINDING SITE FOR RESIDUE SO4 A 211
source : AC4

3) chain A
residue 74
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 212
source : AC5

4) chain A
residue 79
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 A 212
source : AC5

5) chain A
residue 190
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 213
source : AC6

6) chain A
residue 8
type
sequence F
description BINDING SITE FOR RESIDUE GBX A 214
source : AC8

7) chain A
residue 10
type
sequence V
description BINDING SITE FOR RESIDUE GBX A 214
source : AC8

8) chain A
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE GBX A 214
source : AC8

9) chain A
residue 38
type
sequence W
description BINDING SITE FOR RESIDUE GBX A 214
source : AC8

10) chain A
residue 44
type
sequence K
description BINDING SITE FOR RESIDUE GBX A 214
source : AC8

11) chain A
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE GBX A 214
source : AC8

12) chain A
residue 52
type
sequence L
description BINDING SITE FOR RESIDUE GBX A 214
source : AC8

13) chain A
residue 53
type
sequence P
description BINDING SITE FOR RESIDUE GBX A 214
source : AC8

14) chain A
residue 64
type
sequence Q
description BINDING SITE FOR RESIDUE GBX A 214
source : AC8

15) chain A
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE GBX A 214
source : AC8

16) chain A
residue 108
type
sequence Y
description BINDING SITE FOR RESIDUE GBX A 214
source : AC8

17) chain A
residue 205
type
sequence G
description BINDING SITE FOR RESIDUE GBX A 214
source : AC8

18) chain A
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE MES A 215
source : AC9

19) chain A
residue 28
type
sequence W
description BINDING SITE FOR RESIDUE MES A 215
source : AC9

20) chain A
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE MES A 215
source : AC9

21) chain A
residue 197
type
sequence E
description BINDING SITE FOR RESIDUE MES A 215
source : AC9

22) chain A
residue 8
type
sequence F
description BINDING SITE FOR RESIDUE MES A 216
source : BC1

23) chain A
residue 35
type
sequence V
description BINDING SITE FOR RESIDUE MES A 216
source : BC1

24) chain A
residue 38
type
sequence W
description BINDING SITE FOR RESIDUE MES A 216
source : BC1

25) chain A
residue 98
type
sequence D
description BINDING SITE FOR RESIDUE GBX B 213
source : BC2

26) chain A
residue 7
type BINDING
sequence Y
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

27) chain A
residue 13
type BINDING
sequence R
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

28) chain A
residue 38
type BINDING
sequence W
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

29) chain A
residue 44
type BINDING
sequence K
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

30) chain A
residue 51
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

31) chain A
residue 64
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

32) chain A
residue 3
type MOD_RES
sequence Y
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 198
type MOD_RES
sequence Y
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954
source Swiss-Prot : SWS_FT_FI2

34) chain A
residue 61
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

35) chain A
residue 102
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4

36) chain A
residue 115
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P19157
source Swiss-Prot : SWS_FT_FI4

37) chain A
residue 127
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5


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