PDBe 1gp1

X-ray diffraction
2Å resolution

THE REFINED STRUCTURE OF THE SELENOENZYME GLUTATHIONE PEROXIDASE AT 0.2-NM RESOLUTION

Released:
Source organism: Bos taurus

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:
Glutathione peroxidase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 198 amino acids
Theoretical weight: 21.97 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00435 (Residues: 8-205; Coverage: 97%)
Gene name: GPX1
Sequence domains: Glutathione peroxidase
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 90.4Å b: 109.5Å c: 58.2Å
α: 90° β: 99° γ: 90°
R-values:
R R work R free
0.171 0.171 not available
Expression system: Not provided