X-ray diffraction
2.07Å resolution

Crystal structure of bovine lactoperoxidase with a partial Glu258-heme linkage at 2.07 A resolution.

Source organism: Bos taurus
Primary publication:
Structural basis of activation of mammalian heme peroxidases.
Prog. Biophys. Mol. Biol. 133 49-55 (2018)
PMID: 29174286

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (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: 54.012Å b: 79.809Å c: 66.106Å
α: 90° β: 93.01° γ: 90°
R R work R free
0.169 0.167 0.236