X-ray diffraction
1.93Å resolution

Structure of bovine Lactoperoxidase with a partially modified covalent bond with heme moiety

Source organism: Bos taurus
Primary publication:
Structure of bovine lactoperoxidase with a partially linked heme moiety at 1.98Å resolution.
Biochim Biophys Acta Proteins Proteom 1865 329-335 (2017)
PMID: 27986533

Function and Biology Details

Reaction catalysed:
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160329 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lactoperoxidase Chain: A
Molecule details ›
Chain: A
Length: 595 amino acids
Theoretical weight: 67.84 KDa
Source organism: Bos taurus
  • Canonical: P80025 (Residues: 118-712; Coverage: 86%)
Gene name: LPO
Sequence domains: Animal haem peroxidase
Structure domains: Haem peroxidase domain superfamily, animal type

Ligands and Environments

Cofactor: Ligand HEM 1 x HEM
Carbohydrate polymer : NEW Components: NAG
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 54.005Å b: 79.834Å c: 76.126Å
α: 90° β: 102.3° γ: 90°
R R work R free
0.195 0.192 0.245