› 2pdq

X-ray diffraction
1.73Å resolution

Human aldose reductase mutant C303D complexed with uracil-type inhibitor.

Released:
DOI: 10.2210/pdb2pdq/pdb
PDB entry 2pdq coloured by chain, front view.
PDB entry 2pdq coloured by chain, side view.
PDB entry 2pdq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Merging the binding sites of aldose and aldehyde reductase for detection of inhibitor selectivity-determining features.
Steuber H, Heine A, Podjarny A, Klebe G
J Mol Biol 379 991-1016 (2008)
PMID: 18495158

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 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: 35.91 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 NAP 1 x NAP
1 bound ligand:
Ligand 47D 1 x 47D
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P1
Unit cell:
a: 40.32Å b: 47.13Å c: 47.404Å
α: 76.07° β: 67.22° γ: 76.89°
R-values:
R R work R free
0.184 0.182 0.248
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The aldo-keto reductase superfamily and its role in drug metabolism and detoxification.
Barski et al. (2008)
5 more

2 mentions without citation

Small molecule epigenetic inhibitors targeted to histone lysine methyltransferases and demethylases.
Wang et al. (2013)
1 more