› 3zs1

X-ray diffraction
2.6Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138570 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (4 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
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, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
6 bound ligands:
Ligand PVW 2 x PVW
Ligand SO4 3 x SO4
Ligand CA 2 x CA
Ligand CL 2 x CL
Ligand ACT 6 x ACT
Ligand NAG 4 x NAG
1 modified residue:
Ligand CSO 2 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P21
Unit cell:
a: 93.13Å b: 63.79Å c: 111.35Å
α: 90° β: 97.32° γ: 90°
R-values:
R R work R free
0.19 0.187 0.244

Quick links

Citations

21 review citations

Reactive Oxygen Species and Neutrophil Function.
Winterbourn et al. (2016)
20 more

2 mentions without citation

Methods for measuring myeloperoxidase activity toward assessing inhibitor efficacy in living systems.
Huang et al. (2016)
1 more