› 2nvc

X-ray diffraction
1.65Å resolution

Human Aldose Reductase complexed with novel naphtho[1,2-d]isothiazole acetic acid derivative (3)

Released:
DOI: 10.2210/pdb2nvc/pdb
PDB entry 2nvc coloured by chain, front view.
PDB entry 2nvc coloured by chain, side view.
PDB entry 2nvc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Evidence for a novel binding site conformer of aldose reductase in ligand-bound state.
Steuber H, Zentgraf M, La Motta C, Sartini S, Heine A, Klebe G
J Mol Biol 369 186-97 (2007)
PMID: 17418233

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 ITA 1 x ITA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P1
Unit cell:
a: 39.95Å b: 47.09Å c: 46.87Å
α: 76.24° β: 77.16° γ: 67.82°
R-values:
R R work R free
0.16 0.158 0.214
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Limitations and lessons in the use of X-ray structural information in drug design.
Davis et al. (2008)
1 more

1 mention without citation

Path-integral method for predicting relative binding affinities of protein-ligand complexes.
Mulakala et al. (2009)