PDBe 1d2v

X-ray diffraction
1.75Å resolution

CRYSTAL STRUCTURE OF BROMIDE-BOUND HUMAN MYELOPEROXIDASE ISOFORM C AT PH 5.5

Released:

Function and Biology Details

Reaction catalysed:
Cl(-) + H(2)O(2) + H(+) = HClO + H(2)O
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Myeloperoxidase light chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 104 amino acids
Theoretical weight: 11.9 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05164 (Residues: 167-270; Coverage: 15%)
Gene name: MPO
Myeloperoxidase heavy chain Chains: C, D
Molecule details ›
Chains: C, D
Length: 466 amino acids
Theoretical weight: 53.23 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05164 (Residues: 279-744; Coverage: 67%)
Gene name: MPO
Structure domains: Haem peroxidase domain superfamily, animal type

Ligands and Environments

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 111.155Å b: 63.488Å c: 92.476Å
α: 90° β: 97.36° γ: 90°
R-values:
R R work R free
0.243 0.243 0.296