X-ray diffraction
1.5Å resolution

Crystal structure of the selenocysteine to glycine mutant of human glutathione peroxidase 1

Source organism: Homo sapiens
Entry authors: Kavanagh KL, Johansson C, Smee C, Gileadi O, von Delft F, Weigelt J, 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
Glutathione peroxidase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 23.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
  • Canonical: P07203 (Residues: 14-198; Coverage: 91%)
Gene name: GPX1
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: C2
Unit cell:
a: 127.592Å b: 59.376Å c: 81.132Å
α: 90° β: 119.41° γ: 90°
R R work R free
0.138 0.138 0.156
Expression system: Escherichia coli BL21