› 1iei

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF HUMAN ALDOSE REDUCTASE COMPLEXED WITH THE INHIBITOR ZENARESTAT.

Released:
DOI: 10.2210/pdb1iei/pdb
PDB entry 1iei coloured by chain, front view.
PDB entry 1iei coloured by chain, side view.
PDB entry 1iei coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of human recombinant aldose reductase complexed with the potent inhibitor zenarestat.
Kinoshita T, Miyake H, Fujii T, Takakura S, Goto T
Acta Crystallogr D Biol Crystallogr 58 622-6 (2002)
PMID: 11914486

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 NAP 1 x NAP
1 bound ligand:
Ligand ZES 1 x ZES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: P1
Unit cell:
a: 40.4Å b: 47.97Å c: 47.66Å
α: 76.2° β: 76.7° γ: 67.5°
R-values:
R R work R free
0.178 0.178 0.199
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Physiological and Pathological Roles of Aldose Reductase.
Singh et al. (2021)
9 other articles

15 mentions without citation

PLIP: fully automated protein-ligand interaction profiler.
Salentin et al. (2015)
14 more