2he3

X-ray diffraction
2.1Å resolution

Crystal structure of the selenocysteine to cysteine mutant of human glutathionine peroxidase 2 (GPX2)

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

Function and Biology Details

Reactions catalysed:
2 glutathione + a hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H(2)O
2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-148346 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione peroxidase 2 Chain: A
Molecule details ›
Chain: A
Length: 208 amino acids
Theoretical weight: 24.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18283 (Residues: 4-188; Coverage: 97%)
Gene name: GPX2
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: I222
Unit cell:
a: 41.308Å b: 117.212Å c: 120.157Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.156 0.205
Expression system: Escherichia coli