1myp

X-ray diffraction
3Å resolution

X-RAY CRYSTAL STRUCTURE OF CANINE MYELOPEROXIDASE AT 3 ANGSTROMS RESOLUTION

Released:
Source organism: Canis lupus familiaris
Primary publication:
X-ray crystal structure of canine myeloperoxidase at 3 A resolution.
J Mol Biol 226 185-207 (1992)
PMID: 1320128

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

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-138574 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Myeloperoxidase light chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 108 amino acids
Theoretical weight: 12.33 KDa
Source organism: Canis lupus familiaris
Expression system: Not provided
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: Canis lupus familiaris
Expression system: Not provided
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
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 133Å b: 133Å c: 203.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.257 not available not available
Expression system: Not provided