PDBe 2acu

X-ray diffraction
1.76Å resolution

TYROSINE-48 IS THE PROTON DONOR AND HISTIDINE-110 DIRECTS SUBSTRATE STEREOCHEMICAL SELECTIVITY IN THE REDUCTION REACTION OF HUMAN ALDOSE REDUCTASE: ENZYME KINETICS AND THE CRYSTAL STRUCTURE OF THE Y48H MUTANT ENZYME

Released:

Function and Biology Details

Reaction catalysed:
Alditol + NAD(P)(+) = aldose + NAD(P)H
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldose reductase Chain: A
Molecule details ›
Chain: A
Length: 315 amino acids
Theoretical weight: 35.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15121 (Residues: 2-316; Coverage: 100%)
Gene names: AKR1B1, ALDR1
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 49.99Å b: 67.14Å c: 92.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 not available
Expression system: Escherichia coli