› 5zj9

X-ray diffraction
2.6Å resolution

human D-amino acid oxidase complexed with 5-chlorothiophene-3-carboxylic acid

Released:
DOI: 10.2210/pdb5zj9/pdb
PDB entry 5zj9 coloured by chain, front view.
PDB entry 5zj9 coloured by chain, side view.
PDB entry 5zj9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for potent inhibition of d-amino acid oxidase by thiophene carboxylic acids.
Kato Y, Hin N, Maita N, Thomas AG, Kurosawa S, Rojas C, Yorita K, Slusher BS, Fukui K, Tsukamoto T
Eur J Med Chem 159 23-34 (2018)
PMID: 30265959

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: 340 amino acids
Theoretical weight: 38.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14920 (Residues: 1-340; Coverage: 98%)
Gene names: DAMOX, DAO
Sequence domains: FAD dependent oxidoreductase
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD
1 bound ligand:
Ligand 9E6 4 x 9E6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21212
Unit cell:
a: 150.14Å b: 182.73Å c: 51.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.219 0.255
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Structural basis for potent inhibition of d-amino acid oxidase by thiophene carboxylic acids.
Kato et al. (2018)