3erh

X-ray diffraction
2.4Å resolution

First structural evidence of substrate specificity in mammalian peroxidases: Crystal structures of substrate complexes with lactoperoxidases from two different species

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-107648 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Lactoperoxidase Chain: A
Molecule details ›
Chain: A
Length: 595 amino acids
Theoretical weight: 67.9 KDa
Source organism: Bubalus bubalis
UniProt:
  • Canonical: A5JUY8 (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
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer : NEW Components: NAG, MAN, BMA
3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 54.207Å b: 80.541Å c: 77.877Å
α: 90° β: 102.64° γ: 90°
R-values:
R R work R free
0.18 0.18 0.195