› 2qxw

X-ray diffraction
0.8Å resolution

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-147224 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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 NDP 1 x NDP
2 bound ligands:
Ligand LDT 1 x LDT
Ligand CIT 2 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 49.345Å b: 66.945Å c: 47.407Å
α: 90° β: 92.07° γ: 90°
R-values:
R R work R free
0.108 0.104 0.112
Expression system: Escherichia coli

Quick links

Citations

5 review citations

High-throughput crystallography for structural genomics.
Joachimiak A. (2009)
4 more

4 mentions without citation

Quantum model of catalysis based on a mobile proton revealed by subatomic x-ray and neutron diffraction studies of h-aldose reductase.
Blakeley et al. (2008)
3 more