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2GS3

Crystal structure of the selenocysteine to glycine mutant of human glutathione peroxidase 4(GPX4)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 201
ChainResidue
AGLY73
AGLY74
ALYS75
AASN164

Functional Information from PROSITE/UniProt
site_idPS00763
Number of Residues8
DetailsGLUTATHIONE_PEROXID_2 Glutathione peroxidases signature 2. LAFPCNQF
ChainResidueDetails
ALEU98-PHE105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"O70325","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsNon-standard residue: {"description":"Selenocysteine","evidences":[{"source":"PubMed","id":"8039723","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9705830","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P36970","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gp1
ChainResidueDetails
AGLN108
ATRP163

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PDB entries from 2025-11-05

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