3cuk

X-ray diffraction
2.49Å resolution

Crystal structure of human D-amino acid oxidase: bound to an inhibitor

Released:

Function and Biology Details

Reaction catalysed:
A D-amino acid + H(2)O + O(2) = a 2-oxo carboxylate + NH(3) + H(2)O(2)
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147153 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-amino-acid oxidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 347 amino acids
Theoretical weight: 39.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14920 (Residues: 1-347; Coverage: 100%)
Gene names: DAMOX, DAO
Sequence domains: FAD dependent oxidoreductase
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 187.729Å b: 51.145Å c: 153.294Å
α: 90° β: 110.45° γ: 90°
R-values:
R R work R free
0.243 0.239 0.328
Expression system: Escherichia coli BL21(DE3)