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4WR5

Crystal Structure of GST Mutated with Halogenated Tyrosine (7cGST-1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0006749biological_processglutathione metabolic process
A0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue GSH A 301
ChainResidue
ATYR6
ASER67
AASP100
AHOH419
AHOH433
AHOH436
AHOH450
ATRP7
ALEU12
ATRP40
ALYS44
AASN53
ALEU54
APRO55
AGLN66

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 302
ChainResidue
AARG34
AGLY212
AASP213

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 303
ChainResidue
AGLY83
APRO85
AARG88

site_idAC4
Number of Residues12
Detailsbinding site for Ligand residues 3CT A 0 through SER A 1 bound to SER A -1
ChainResidue
ASER-1
APRO2
AILE3
ALYS26
AGLU28
AILE58
AASP59
AGLY60
APRO126
AGLU127
AHOH404
AHOH431

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7538846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12596270","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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