PDBe 3f9p

X-ray diffraction
2.93Å resolution

Crystal structure of myeloperoxidase from human leukocytes

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Myeloperoxidase light chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 114 amino acids
Theoretical weight: 12.89 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05164 (Residues: 165-278; Coverage: 16%)
Gene name: MPO
Myeloperoxidase heavy chain Chains: C, D
Molecule details ›
Chains: C, D
Length: 467 amino acids
Theoretical weight: 53.32 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05164 (Residues: 279-745; Coverage: 67%)
Gene name: MPO
Structure domains: Haem peroxidase domain superfamily, animal type

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P43212
Unit cell:
a: 110.74Å b: 110.74Å c: 255.333Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.236 0.257