eF-site ID 4wr5-A
PDB Code 4wr5
Chain A

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Title Crystal Structure of GST Mutated with Halogenated Tyrosine (7cGST-1)
Classification TRANSFERASE
Compound Glutathione S-transferase class-mu 26 kDa isozyme
Source (GST26_SCHJA)
Sequence A:  SXSPILGYWKIKGLVQPTRLLLEXLEEKYEEHLXERDEGD
KWRNKKFELGLEFPNLPYXIDGDVKLTQSMAIIRXIADKH
NMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLK
VDFLSKLPEMLKMFEDRLCHKTXLNGDHVTHPDFMLYDAL
DVVLXMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYI
AWPLQGWQATFGGGDHPP
Description


Functional site

1) chain A
residue 6
type
sequence Y
description binding site for residue GSH A 301
source : AC1

2) chain A
residue 7
type
sequence W
description binding site for residue GSH A 301
source : AC1

3) chain A
residue 12
type
sequence L
description binding site for residue GSH A 301
source : AC1

4) chain A
residue 40
type
sequence W
description binding site for residue GSH A 301
source : AC1

5) chain A
residue 44
type
sequence K
description binding site for residue GSH A 301
source : AC1

6) chain A
residue 53
type
sequence N
description binding site for residue GSH A 301
source : AC1

7) chain A
residue 54
type
sequence L
description binding site for residue GSH A 301
source : AC1

8) chain A
residue 55
type
sequence P
description binding site for residue GSH A 301
source : AC1

9) chain A
residue 66
type
sequence Q
description binding site for residue GSH A 301
source : AC1

10) chain A
residue 67
type
sequence S
description binding site for residue GSH A 301
source : AC1

11) chain A
residue 100
type
sequence D
description binding site for residue GSH A 301
source : AC1

12) chain A
residue 34
type
sequence R
description binding site for residue SO4 A 302
source : AC2

13) chain A
residue 212
type
sequence G
description binding site for residue SO4 A 302
source : AC2

14) chain A
residue 213
type
sequence D
description binding site for residue SO4 A 302
source : AC2

15) chain A
residue 83
type
sequence G
description binding site for residue SO4 A 303
source : AC3

16) chain A
residue 85
type
sequence P
description binding site for residue SO4 A 303
source : AC3

17) chain A
residue 88
type
sequence R
description binding site for residue SO4 A 303
source : AC3

18) chain A
residue -1
type
sequence S
description binding site for Ligand residues 3CT A 0 through SER A 1 bound to SER A -1
source : AC4

19) chain A
residue 2
type
sequence P
description binding site for Ligand residues 3CT A 0 through SER A 1 bound to SER A -1
source : AC4

20) chain A
residue 3
type
sequence I
description binding site for Ligand residues 3CT A 0 through SER A 1 bound to SER A -1
source : AC4

21) chain A
residue 26
type
sequence K
description binding site for Ligand residues 3CT A 0 through SER A 1 bound to SER A -1
source : AC4

22) chain A
residue 28
type
sequence E
description binding site for Ligand residues 3CT A 0 through SER A 1 bound to SER A -1
source : AC4

23) chain A
residue 58
type
sequence I
description binding site for Ligand residues 3CT A 0 through SER A 1 bound to SER A -1
source : AC4

24) chain A
residue 59
type
sequence D
description binding site for Ligand residues 3CT A 0 through SER A 1 bound to SER A -1
source : AC4

25) chain A
residue 60
type
sequence G
description binding site for Ligand residues 3CT A 0 through SER A 1 bound to SER A -1
source : AC4

26) chain A
residue 126
type
sequence P
description binding site for Ligand residues 3CT A 0 through SER A 1 bound to SER A -1
source : AC4

27) chain A
residue 127
type
sequence E
description binding site for Ligand residues 3CT A 0 through SER A 1 bound to SER A -1
source : AC4

28) chain A
residue 6
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270
source Swiss-Prot : SWS_FT_FI1

29) chain A
residue 40
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270
source Swiss-Prot : SWS_FT_FI1

30) chain A
residue 53
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270
source Swiss-Prot : SWS_FT_FI1

31) chain A
residue 66
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 110
type BINDING
sequence Y
description BINDING => ECO:0000305
source Swiss-Prot : SWS_FT_FI2


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