5l71

X-ray diffraction
1.8Å resolution

Crystal structure of mouse phospholipid hydroperoxide glutathione peroxidase 4 (GPx4)

Released:
Source organism: Mus musculus
Primary publication:
Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4.
Acta Crystallogr F Struct Biol Commun 72 743-749 (2016)
PMID: 27710939

Function and Biology Details

Reactions catalysed:
2 glutathione + a hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H(2)O
2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-130690 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipid hydroperoxide glutathione peroxidase GPX4 Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 19.56 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: O70325 (Residues: 29-197; Coverage: 86%)
Gene name: Gpx4
Sequence domains: Glutathione peroxidase
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3121
Unit cell:
a: 61.26Å b: 61.26Å c: 113.98Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.153 0.151 0.193
Expression system: Escherichia coli