› 1c0p

X-ray diffraction
1.2Å resolution

D-AMINO ACIC OXIDASE IN COMPLEX WITH D-ALANINE AND A PARTIALLY OCCUPIED BIATOMIC SPECIES

Released:
DOI: 10.2210/pdb1c0p/pdb
PDB entry 1c0p coloured by chain, front view.
PDB entry 1c0p coloured by chain, side view.
PDB entry 1c0p coloured by chain, top view.
Source organism: Rhodotorula toruloides
Primary publication:
The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation.
Umhau S, Pollegioni L, Molla G, Diederichs K, Welte W, Pilone MS, Ghisla S
Proc Natl Acad Sci U S A 97 12463-8 (2000)
PMID: 11070076

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:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160390 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-amino-acid oxidase Chain: A
Molecule details ›
Chain: A
Length: 363 amino acids
Theoretical weight: 39.61 KDa
Source organism: Rhodotorula toruloides
Expression system: Escherichia coli
UniProt:
  • Canonical: P80324 (Residues: 1-361; Coverage: 98%)
Gene name: DAO1
Sequence domains: FAD dependent oxidoreductase
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
3 bound ligands:
Ligand DAL 1 x DAL
Ligand PER 1 x PER
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: I422
Unit cell:
a: 120.885Å b: 120.885Å c: 136.364Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.125 not available 0.15
Expression system: Escherichia coli

Quick links

Citations

21 review citations

To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes.
Mattevi A. (2006)
20 more

10 mentions without citation

The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation.
Umhau et al. (2000)
9 more