› 1pr9

X-ray diffraction
1.96Å resolution

Human L-Xylulose Reductase Holoenzyme

Released:
DOI: 10.2210/pdb1pr9/pdb
PDB entry 1pr9 coloured by chain, front view.
PDB entry 1pr9 coloured by chain, side view.
PDB entry 1pr9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis.
El-Kabbani O, Ishikura S, Darmanin C, Carbone V, Chung RP, Usami N, Hara A
Proteins 55 724-32 (2004)
PMID: 15103634

Function and Biology Details

Reaction catalysed: 
Xylitol + NADP(+) = L-xylulose + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-182274 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-xylulose reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 244 amino acids
Theoretical weight: 25.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q7Z4W1 (Residues: 1-244; Coverage: 100%)
Gene names: DCXR, SDR20C1
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAP 2 x NAP
2 bound ligands:
Ligand K 2 x K
Ligand 2HP 2 x 2HP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21212
Unit cell:
a: 74.111Å b: 87.938Å c: 72.883Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.227
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Human DCXR - another 'moonlighting protein' involved in sugar metabolism, carbonyl detoxification, cell adhesion and male fertility?
Ebert et al. (2015)
2 more

3 mentions without citation

Structure/function of human type 1 3beta-hydroxysteroid dehydrogenase: An intrasubunit disulfide bond in the Rossmann-fold domain and a Cys residue in the active site are critical for substrate and coenzyme utilization.
Thomas et al. (2007)
2 more