› 1mi3

X-ray diffraction
1.8Å resolution

1.8 Angstrom structure of xylose reductase from Candida tenuis in complex with NAD

Released:
DOI: 10.2210/pdb1mi3/pdb
PDB entry 1mi3 coloured by chain, front view.
PDB entry 1mi3 coloured by chain, side view.
PDB entry 1mi3 coloured by chain, top view.
Source organism: Yamadazyma tenuis
Primary publication:
Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases.
Kavanagh KL, Klimacek M, Nidetzky B, Wilson DK
Biochem J 373 319-26 (2003)
PMID: 12733986

Function and Biology Details

Reaction catalysed: 
Xylitol + NAD(P)(+) = D-xylose + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-130775 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD(P)H-dependent D-xylose reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 322 amino acids
Theoretical weight: 36.06 KDa
Source organism: Yamadazyma tenuis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O74237 (Residues: 1-322; Coverage: 100%)
Gene names: XYL1, XYLR
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: C2
Unit cell:
a: 180.202Å b: 128.344Å c: 79.949Å
α: 90° β: 90.75° γ: 90°
R-values:
R R work R free
0.183 0.183 0.212
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Ethanol production from xylose in engineered Saccharomyces cerevisiae strains: current state and perspectives.
Matsushika et al. (2009)
5 more

17 mentions without citation

The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography.
Petschacher et al. (2005)
16 more