› 4ysw

X-ray diffraction
1.99Å resolution

Structure of rat xanthine oxidoreductase, C-terminal deletion protein variant, NADH bound form

Released:
DOI: 10.2210/pdb4ysw/pdb
PDB entry 4ysw coloured by chain, front view.
PDB entry 4ysw coloured by chain, side view.
PDB entry 4ysw coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The C-terminal peptide plays a role in the formation of an intermediate form during the transition between xanthine dehydrogenase and xanthine oxidase.
Nishino T, Okamoto K, Kawaguchi Y, Matsumura T, Eger BT, Pai EF, Nishino T
OpenAccess logo FEBS J 282 3075-90 (2015)
PMID: 25817260

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

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149853 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xanthine dehydrogenase/oxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 1315 amino acids
Theoretical weight: 144.65 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P22985 (Residues: 1-1315; Coverage: 99%)
Gene name: Xdh
Sequence domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand NAI 2 x NAI
5 bound ligands:
Ligand FES 4 x FES
Ligand CA 2 x CA
Ligand BCT 2 x BCT
Ligand URC 2 x URC
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 98.46Å b: 137.643Å c: 222.067Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.219
Expression system: Spodoptera frugiperda

Quick links

Citations

13 review citations

NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential.
Xie et al. (2020)
12 more

1 mention without citation

The C-terminal peptide plays a role in the formation of an intermediate form during the transition between xanthine dehydrogenase and xanthine oxidase.
Nishino et al. (2015)