PDBe 1mhl

X-ray diffraction
2.25Å resolution

CRYSTAL STRUCTURE OF HUMAN MYELOPEROXIDASE ISOFORM C CRYSTALLIZED IN SPACE GROUP P2(1) AT PH 5.5 AND 20 DEG C

Released:
Source organism: Homo sapiens
Primary publication:
Structure of the green heme in myeloperoxidase.
Arch. Biochem. Biophys. 316 653-6 (1995)
PMID: 7840679

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: 108 amino acids
Theoretical weight: 12.33 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05164 (Residues: 165-272; Coverage: 16%)
Gene name: MPO
Myeloperoxidase heavy chain Chains: C, D
Molecule details ›
Chains: C, D
Length: 466 amino acids
Theoretical weight: 53.22 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

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 111.7Å b: 64.6Å c: 94.2Å
α: 90° β: 97.9° γ: 90°
R-values:
R R work R free
0.16 0.16 not available