6elw

X-ray diffraction
1.3Å resolution

High resolution structure of selenocysteine containing human GPX4

Released:

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-153272 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipid hydroperoxide glutathione peroxidase GPX4 Chain: A
Molecule details ›
Chain: A
Length: 192 amino acids
Theoretical weight: 21.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P36969 (Residues: 29-197; Coverage: 86%)
Gene name: GPX4
Sequence domains: Glutathione peroxidase
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 32.963Å b: 69Å c: 35.666Å
α: 90° β: 115.12° γ: 90°
R-values:
R R work R free
0.125 0.124 0.155
Expression system: Escherichia coli BL21(DE3)