1prx

X-ray diffraction
2Å resolution

HORF6 A NOVEL HUMAN PEROXIDASE ENZYME

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution.
Nat. Struct. Biol. 5 400-6 (1998)
PMID: 9587003

Function and Biology Details

Reactions catalysed:
2 glutathione + ROOH = glutathione disulfide + H(2)O + ROH
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate
Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxiredoxin-6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 224 amino acids
Theoretical weight: 25.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30041 (Residues: 1-224; Coverage: 100%)
Gene names: AOP2, KIAA0106, PRDX6
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 47.85Å b: 75.17Å c: 63.3Å
α: 90° β: 110.21° γ: 90°
R-values:
R R work R free
0.191 0.191 0.259
Expression system: Escherichia coli