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5L71

Crystal structure of mouse phospholipid hydroperoxide 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 Residues7
Detailsbinding site for residue EDO A 201
ChainResidue
AASN109
AGLY110
ALYS121
AALA133
AHOH360
AHOH382
AHOH429

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 202
ChainResidue
AARG69
AHOH307
ALYS31
APHE35

site_idAC3
Number of Residues8
Detailsbinding site for residue EDO A 203
ChainResidue
ACYS10
ASER44
AGLN45
AGLU88
APHE92
AHOH329
AHOH351
AHOH449

Functional Information from PROSITE/UniProt
site_idPS00460
Number of Residues16
DetailsGLUTATHIONE_PEROXID_1 Glutathione peroxidases active site. GFvCIVtNVaSqCGkT
ChainResidueDetails
AGLY34-THR49

site_idPS00763
Number of Residues8
DetailsGLUTATHIONE_PEROXID_2 Glutathione peroxidases signature 2. LAFPCNQF
ChainResidueDetails
ALEU71-PHE78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:29290465
ChainResidueDetails
ACYS46

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P36970
ChainResidueDetails
ASER13

224004

PDB entries from 2024-08-21

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