PDBe 3kij

X-ray diffraction
1.8Å resolution

Crystal structure of the human PDI-peroxidase

Released:

Function and Biology Details

Reaction catalysed:
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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable glutathione peroxidase 8 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 180 amino acids
Theoretical weight: 21.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TED1 (Residues: 38-209; Coverage: 82%)
Gene names: GPX8, UNQ847/PRO1785
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: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: C2
Unit cell:
a: 90.43Å b: 122.3Å c: 70.18Å
α: 90° β: 117.9° γ: 90°
R-values:
R R work R free
0.211 0.209 0.248
Expression system: Escherichia coli