PDBe 4ejx

X-ray diffraction
4.69Å resolution

Structure of ceruloplasmin-myeloperoxidase complex

Released:

Function and Biology Details

Reactions catalysed:
4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O
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 trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ceruloplasmin Chain: A
Molecule details ›
Chain: A
Length: 1065 amino acids
Theoretical weight: 122.34 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00450 (Residues: 1-1065; Coverage: 100%)
Gene name: CP
Sequence domains:
Myeloperoxidase light chain Chain: B
Molecule details ›
Chain: 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 Chain: D
Molecule details ›
Chain: D
Length: 467 amino acids
Theoretical weight: 53.31 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05164 (Residues: 279-745; Coverage: 67%)
Gene name: MPO

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P6522
Unit cell:
a: 106.249Å b: 106.249Å c: 834.619Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.367 0.366 0.401