4gac

X-ray diffraction
1.64Å resolution

High resolution structure of mouse aldehyde reductase (AKR1a4) in its apo-form

Released:
Source organism: Mus musculus
Primary publication:
High-resolution structure of AKR1a4 in the apo form and its interaction with ligands.
Acta Crystallogr Sect F Struct Biol Cryst Commun 68 1271-4 (2012)
PMID: 23143230

Function and Biology Details

Reactions catalysed:
L-gulonate + NADP(+) = D-glucuronate + NADPH
An alcohol + NADP(+) = an aldehyde + NADPH
L-gulono-1,4-lactone + NADP(+) = D-glucurono-3,6-lactone + NADPH
Glycerol + NADP(+) = D-glyceraldehyde + NADPH
Allyl alcohol + NADP(+) = acrolein + NADPH

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-191606 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldo-keto reductase family 1 member A1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 324 amino acids
Theoretical weight: 36.51 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9JII6 (Residues: 2-325; Coverage: 100%)
Gene names: Akr1a1, Akr1a4
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21
Unit cell:
a: 56.94Å b: 92.62Å c: 70.1Å
α: 90° β: 106.16° γ: 90°
R-values:
R R work R free
0.15 0.148 0.178
Expression system: Escherichia coli BL21(DE3)