3gcl

X-ray diffraction
2.5Å resolution

Mode of ligand binding and assignment of subsites in mammalian peroxidases: crystal structure of lactoperoxidase complexes with acetyl salycylic acid, salicylhydroxamic acid and benzylhydroxamic acid

Released:

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: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 54.66Å b: 80.52Å c: 77.97Å
α: 90° β: 102.65° γ: 90°
R-values:
R R work R free
0.201 0.201 0.223