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3GX0

Crystal Structure of GSH-dependent Disulfide bond Oxidoreductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0004601molecular_functionperoxidase activity
A0005737cellular_componentcytoplasm
A0006979biological_processresponse to oxidative stress
A0015036molecular_functiondisulfide oxidoreductase activity
A0016491molecular_functionoxidoreductase activity
A0042803molecular_functionprotein homodimerization activity
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GDS A 301
ChainResidue
ATHR9
APRO110
AGLY113
AARG132
ATRP169
AHOH220
AHOH271
AHOH272
AHOH273
AHOH289
AHOH297
AASN11
AGLN38
AASN50
ALYS51
AILE52
AGLU71
ASER72
AGLY109

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues86
DetailsDomain: {"description":"GST N-terminal"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19537707","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P08263","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR5

242500

PDB entries from 2025-10-01

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