2r37

X-ray diffraction
1.85Å resolution

Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine mutant)

Released:
Source organism: Homo sapiens
Entry authors: Pilka ES, Guo K, Gileadi O, Rojkowa A, von Delft F, Pike ACW, Kavanagh KL, Johannson C, Sundstrom M, Arrowsmith CH, Weigelt J, Edwards AM, 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

Assemblies composition:
homo dimer (preferred)
homo tetramer
PDBe Complex ID:
PDB-CPX-149602 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione peroxidase 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 207 amino acids
Theoretical weight: 23.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22352 (Residues: 25-223; Coverage: 97%)
Gene names: GPX3, GPXP
Sequence domains: Glutathione peroxidase
Structure domains: Glutaredoxin

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21212
Unit cell:
a: 103.72Å b: 61.308Å c: 100.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 0.151 0.183
Expression system: Escherichia coli