› 3q67

X-ray diffraction
1.55Å resolution

Human Aldose Reductase C298S mutant in Complex with NADP+ in Space Group P212121

Released:
DOI: 10.2210/pdb3q67/pdb
PDB entry 3q67 coloured by chain, front view.
PDB entry 3q67 coloured by chain, side view.
PDB entry 3q67 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The role of Cys-298 in aldose reductase function.
Balendiran GK, Sawaya MR, Schwarz FP, Ponniah G, Cuckovich R, Verma M, Cascio D
J Biol Chem 286 6336-44 (2011)
PMID: 21084309

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 316 amino acids
Theoretical weight: 35.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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 2 x NAP
1 bound ligand:
Ligand SO4 8 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 83.728Å b: 86.178Å c: 104.382Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.189
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.
Ghai et al. (2012)
2 more

2 mentions without citation

The role of Cys-298 in aldose reductase function.
Balendiran et al. (2011)
1 more