› 3g3e

X-ray diffraction
2.2Å resolution

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:
Biological process:
Cellular component:
Sequence domains:

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: 351 amino acids
Theoretical weight: 39.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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:
Ligand G3E 4 x G3E
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P1
Unit cell:
a: 51.063Å b: 82.584Å c: 96.974Å
α: 102.62° β: 105.43° γ: 110.79°
R-values:
R R work R free
0.242 0.239 0.294
Expression system: Escherichia coli

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Citations

13 review citations

Carboxylic acid (bio)isosteres in drug design.
Ballatore et al. (2013)
12 more

4 mentions without citation

Competitive Inhibitors Unveil Structure/Function Relationships in Human D-Amino Acid Oxidase.
Molla G. (2017)
3 more