1d7w

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF HUMAN MYELOPEROXIDASE ISOFORM C COMPLEXED WITH CYANIDE AND BROMIDE AT PH 4.0

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-138570 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 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
Sequence domains: Animal haem peroxidase
Structure domains: Haem peroxidase domain superfamily, animal type

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 111.338Å b: 63.324Å c: 92.263Å
α: 90° β: 97.41° γ: 90°
R-values:
R R work R free
0.215 0.215 0.27