3gck

X-ray diffraction
2.9Å 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:
Source organism: Bos taurus
Entry authors: Singh AK, Singh N, Sinha M, Bhushan A, Kaur P, Srinivasan A, 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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
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
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer : NEW Components: NAG
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 54.515Å b: 80.113Å c: 68.571Å
α: 90° β: 93.99° γ: 90°
R-values:
R R work R free
0.199 0.199 0.224