2i3y

X-ray diffraction
2Å resolution

Crystal structure of human glutathione peroxidase 5

Released:
Source organism: Homo sapiens
Entry authors: Kavanagh KL, Johansson C, Rojkova A, Umeano C, Bunkoczi G, Gileadi O, von Delft F, Weigelt J, Arrowsmith C, Sundstrom M, Edwards A, Oppermann U, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epididymal secretory glutathione peroxidase Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 24.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O75715 (Residues: 28-220; Coverage: 97%)
Gene name: GPX5
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 X10SA
Spacegroup: P6222
Unit cell:
a: 104.544Å b: 104.544Å c: 71.663Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.175 0.228
Expression system: Escherichia coli BL21(DE3)