2pt3

X-ray diffraction
2.34Å resolution

Crystal structure of bovine lactoperoxidase at 2.34 A resolution reveals multiple anion binding sites

Released:
Source organism: Bos taurus
Entry authors: Singh AK, Singh N, Sharma S, Kaur P, Betzel C, Singh TP

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lactoperoxidase Chain: A
Molecule details ›
Chain: A
Length: 595 amino acids
Theoretical weight: 67.85 KDa
Source organism: Bos taurus
UniProt:
  • 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

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21
Unit cell:
a: 53.91Å b: 80.051Å c: 75.675Å
α: 90° β: 103.23° γ: 90°
R-values:
R R work R free
0.232 0.231 0.247