› 2qqt

X-ray diffraction
2.5Å resolution

Crystal structure of the complex of bovine lactoperoxidase with acetyl salicylic acid at 2.5 A resolution

Released:
DOI: 10.2210/pdb2qqt/pdb
PDB 2qqt coloured by chain and viewed from the front.
PDB 2qqt coloured by chain and viewed from the side.
PDB 2qqt coloured by chain and viewed from the top.
Source organism: Bos taurus
Entry authors: Singh AK, Singh N, Sharma S, Kaur P, 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
Sequence domains:

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
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
4 bound ligands:
Ligand AIN 1 x AIN
Ligand CA 1 x CA
Ligand SCN 1 x SCN
Ligand IOD 7 x IOD
1 modified residue:
Ligand SEP 1 x SEP

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
0.2 0.194 0.211

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