X-ray diffraction
1.07Å resolution

Human Aldose Reductase mutant T113V in complex with Zopolrestat

Source organism: Homo sapiens
Primary publication:
Ligand-induced fit affects binding modes and provokes changes in crystal packing of aldose reductase.
Biochim. Biophys. Acta 1810 879-87 (2011)
PMID: 21684320

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
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Aldo-keto reductase family 1 member B1 Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 35.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P15121 (Residues: 1-316; Coverage: 100%)
Gene names: AKR1B1, ALDR1, ALR2
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments

Cofactor: Ligand NAP 1 x NAP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P1
Unit cell:
a: 40.04Å b: 47.03Å c: 47.4Å
α: 76.19° β: 67.5° γ: 77.34°
R R work R free
0.116 not available 0.145
Expression system: Escherichia coli