X-ray diffraction
1.98Å resolution

Structure of the lactoperoxidase with bound nitric oxide and nitrite in the substrate binding site at 1.98 A resolution.

Source organism: Capra hircus
Entry authors: Viswanathan V, Kumar M, Singh RP, Singh AK, Sinha M, Kaur P, Sharma P, Sharma S, 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:
  • 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: 67.65 KDa
Source organism: Capra hircus
  • Canonical: A0A452E9Y6 (Residues: 118-712; Coverage: 86%)
Gene name: LPO
Sequence domains: Animal haem peroxidase

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: 54.052Å b: 80.342Å c: 76.121Å
α: 90° β: 102.82° γ: 90°
R R work R free
0.179 0.176 0.235