eF-site ID 5ddl-A
PDB Code 5ddl
Chain A

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Title Crystal Structure of WT Human Glutathione Transferase Pi soaked with a metalloid then back-soaked with glutathione
Classification TRANSFERASE
Compound Glutathione S-transferase P
Source Homo sapiens (Human) (GSTP1_HUMAN)
Sequence A:  MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQ
EGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLY
GKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYV
KALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLL
LIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYV
NLPINGNGKQ
Description


Functional site

1) chain A
residue 22
type
sequence A
description binding site for residue MES A 301
source : AC1

2) chain A
residue 28
type
sequence W
description binding site for residue MES A 301
source : AC1

3) chain A
residue 30
type
sequence E
description binding site for residue MES A 301
source : AC1

4) chain A
residue 197
type
sequence E
description binding site for residue MES A 301
source : AC1

5) chain A
residue 8
type
sequence F
description binding site for residue 5AU A 302
source : AC2

6) chain A
residue 13
type
sequence R
description binding site for residue 5AU A 302
source : AC2

7) chain A
residue 38
type
sequence W
description binding site for residue 5AU A 302
source : AC2

8) chain A
residue 44
type
sequence K
description binding site for residue 5AU A 302
source : AC2

9) chain A
residue 50
type
sequence G
description binding site for residue 5AU A 302
source : AC2

10) chain A
residue 51
type
sequence Q
description binding site for residue 5AU A 302
source : AC2

11) chain A
residue 52
type
sequence L
description binding site for residue 5AU A 302
source : AC2

12) chain A
residue 53
type
sequence P
description binding site for residue 5AU A 302
source : AC2

13) chain A
residue 64
type
sequence Q
description binding site for residue 5AU A 302
source : AC2

14) chain A
residue 65
type
sequence S
description binding site for residue 5AU A 302
source : AC2

15) chain A
residue 104
type
sequence I
description binding site for residue 5AU A 302
source : AC2

16) chain A
residue 108
type
sequence Y
description binding site for residue 5AU A 302
source : AC2

17) chain A
residue 7
type
sequence Y
description binding site for residue GSH A 303
source : AC3

18) chain A
residue 8
type
sequence F
description binding site for residue GSH A 303
source : AC3

19) chain A
residue 13
type
sequence R
description binding site for residue GSH A 303
source : AC3

20) chain A
residue 38
type
sequence W
description binding site for residue GSH A 303
source : AC3

21) chain A
residue 44
type
sequence K
description binding site for residue GSH A 303
source : AC3

22) chain A
residue 50
type
sequence G
description binding site for residue GSH A 303
source : AC3

23) chain A
residue 51
type
sequence Q
description binding site for residue GSH A 303
source : AC3

24) chain A
residue 52
type
sequence L
description binding site for residue GSH A 303
source : AC3

25) chain A
residue 53
type
sequence P
description binding site for residue GSH A 303
source : AC3

26) chain A
residue 64
type
sequence Q
description binding site for residue GSH A 303
source : AC3

27) chain A
residue 65
type
sequence S
description binding site for residue GSH A 303
source : AC3

28) chain A
residue 98
type
sequence D
description binding site for residue 5AU B 303
source : AC6

29) chain A
residue 98
type
sequence D
description binding site for residue GSH B 304
source : AC7

30) chain A
residue 171
type
sequence D
description binding site for residue CA B 306
source : AC9

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

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

33) 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

34) 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

35) 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

36) 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

37) 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

38) 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

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

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

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

42) 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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