› 2obi

X-ray diffraction
1.55Å resolution

Crystal structure of the Selenocysteine to Cysteine Mutant of human phospholipid hydroperoxide glutathione peroxidase (GPx4)

Released:
DOI: 10.2210/pdb2obi/pdb
PDB entry 2obi coloured by chain, front view.
PDB entry 2obi coloured by chain, side view.
PDB entry 2obi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for catalytic activity and enzyme polymerization of phospholipid hydroperoxide glutathione peroxidase-4 (GPx4).
Scheerer P, Borchert A, Krauss N, Wessner H, Gerth C, Höhne W, Kuhn H
Biochemistry 46 9041-9 (2007)
PMID: 17630701

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
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: 183 amino acids
Theoretical weight: 20.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36969 (Residues: 29-197; Coverage: 86%)
Gene name: GPX4
Sequence domains: Glutathione peroxidase
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P3121
Unit cell:
a: 61.362Å b: 61.362Å c: 113.891Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.164 0.186
Expression system: Escherichia coli

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Citations

14 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
13 more

18 mentions without citation

Peroxidation of polyunsaturated fatty acids by lipoxygenases drives ferroptosis.
Yang et al. (2016)
17 more