› 1dla

X-ray diffraction
3Å resolution

NOVEL NADPH-BINDING DOMAIN REVEALED BY THE CRYSTAL STRUCTURE OF ALDOSE REDUCTASE

Released:
DOI: 10.2210/pdb1dla/pdb
PDB entry 1dla coloured by chain, front view.
PDB entry 1dla coloured by chain, side view.
PDB entry 1dla coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Novel NADPH-binding domain revealed by the crystal structure of aldose reductase.
Rondeau JM, Tête-Favier F, Podjarny A, Reymann JM, Barth P, Biellmann JF, Moras D
Nature 355 469-72 (1992)
PMID: 1734286

Function and Biology Details

Reactions catalysed: 
Alditol + NAD(P)(+) = aldose + NAD(P)H
All-trans-retinol + NADP(+) = all-trans-retinal + NADPH
Glycerol + NADP(+) = D-glyceraldehyde + NADPH
Allyl alcohol + NADP(+) = acrolein + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160380 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldo-keto reductase family 1 member B1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 314 amino acids
Theoretical weight: 35.71 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P80276 (Residues: 3-316; Coverage: 99%)
Gene names: AKR1B1, ALR2
Sequence domains: Aldo/keto reductase family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 81.3Å b: 85.9Å c: 56.6Å
α: 102.3° β: 103.3° γ: 79°
R-values:
R R work R free
0.219 0.219 not available
Expression system: Not provided

Quick links

Citations

12 review citations

Comparative anatomy of the aldo-keto reductase superfamily.
Jez et al. (1997)
11 more

3 mentions without citation

Toward a resolution of the introns early/late debate: only phase zero introns are correlated with the structure of ancient proteins.
de Souza et al. (1998)
2 more