› 1wyg

X-ray diffraction
2.6Å resolution

Crystal Structure of a Rat Xanthine Dehydrogenase Triple Mutant (C535A, C992R and C1324S)

Released:
DOI: 10.2210/pdb1wyg/pdb
PDB entry 1wyg coloured by chain, front view.
PDB entry 1wyg coloured by chain, side view.
PDB entry 1wyg coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Mechanism of the conversion of xanthine dehydrogenase to xanthine oxidase: identification of the two cysteine disulfide bonds and crystal structure of a non-convertible rat liver xanthine dehydrogenase mutant.
Nishino T, Okamoto K, Kawaguchi Y, Hori H, Matsumura T, Eger BT, Pai EF, Nishino T
J Biol Chem 280 24888-94 (2005)
PMID: 15878860

Function and Biology Details

Reactions catalysed: 
Xanthine + NAD(+) + H(2)O = urate + NADH
Xanthine + H(2)O + O(2) = urate + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-149852 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xanthine dehydrogenase/oxidase Chain: A
Molecule details ›
Chain: A
Length: 1331 amino acids
Theoretical weight: 146.42 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P22985 (Residues: 1-1331; Coverage: 100%)
Gene name: Xdh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
5 bound ligands:
Ligand PO4 3 x PO4
Ligand CA 1 x CA
Ligand FES 2 x FES
Ligand SAL 1 x SAL
Ligand ACY 1 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: I4122
Unit cell:
a: 134.253Å b: 134.253Å c: 523.315Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.248
Expression system: Spodoptera frugiperda

Quick links

Citations

26 review citations

Therapeutic effects of xanthine oxidase inhibitors: renaissance half a century after the discovery of allopurinol.
Pacher et al. (2006)
25 more

4 mentions without citation

Association of Mutations Identified in Xanthinuria with the Function and Inhibition Mechanism of Xanthine Oxidoreductase.
Sekine et al. (2021)
3 more