PDBe 5fiw

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF HUMAN MYELOPEROXIDASE AT 1.7 ANGSTROMS RESOLUTION

Released:
Source organism: Homo sapiens
Entry authors: Bonnefond L, Cavarelli J

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: 105 amino acids
Theoretical weight: 11.97 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05164 (Residues: 167-271; 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


Cofactor: Ligand HEM 2 x HEM

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P43212
Unit cell:
a: 105.16Å b: 105.16Å c: 225.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.163 0.193