› 2i17

X-ray diffraction
0.81Å resolution

Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 60K

Released:
DOI: 10.2210/pdb2i17/pdb
PDB entry 2i17 coloured by chain, front view.
PDB entry 2i17 coloured by chain, side view.
PDB entry 2i17 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Ultrahigh-resolution study of protein atomic displacement parameters at cryotemperatures obtained with a helium cryostat.
Petrova T, Ginell S, Mitschler A, Hazemann I, Schneider T, Cousido A, Lunin VY, Joachimiak A, Podjarny A
Acta Crystallogr D Biol Crystallogr 62 1535-44 (2006)
PMID: 17139089

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: 49.214Å b: 66.701Å c: 47.307Å
α: 90° β: 92.27° γ: 90°
R-values:
R R work R free
0.081 0.076 0.091
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Could MM-GBSA be accurate enough for calculation of absolute protein/ligand binding free energies?
Mulakala et al. (2013)
7 more

1 mention without citation

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