X-ray diffraction
1.9Å resolution

Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of C. beijerinckii ADH by T. brockii ADH


Function and Biology Details

Reaction catalysed:
Propan-2-ol + NADP(+) = acetone + NADPH
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
NADP-dependent isopropanol dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 351 amino acids
Theoretical weight: 37.65 KDa
Source organisms: Expression system: Escherichia coli
  • Canonical: P25984 (Residues: 8-164, 302-351; Coverage: 59%)
  • Canonical: P14941 (Residues: 1-7, 165-301; Coverage: 41%)
Gene name: adh
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: I23
Unit cell:
a: 129.477Å b: 129.477Å c: 129.477Å
α: 90° β: 90° γ: 90°
R R work R free
0.125 0.122 0.172
Expression system: Escherichia coli