3cmi

X-ray diffraction
2.02Å resolution

Crystal structure of glutathione-dependent phospholipid peroxidase Hyr1 from the yeast Saccharomyces cerevisiae

Released:

Function and Biology Details

Reaction catalysed:
Thioredoxin + ROOH = thioredoxin disulfide + H(2)O + ROH
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-154150 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione peroxidase-like peroxiredoxin HYR1 Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 19.68 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P40581 (Residues: 1-163; Coverage: 100%)
Gene names: GPX3, HYR1, ORP1, YIR037W
Sequence domains: Glutathione peroxidase
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 39.57Å b: 64.88Å c: 72.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.224 0.256
Expression system: Escherichia coli