X-ray diffraction
2.2Å resolution

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


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
NADP-dependent isopropanol dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 352 amino acids
Theoretical weight: 37.81 KDa
Source organisms: Expression system: Escherichia coli
  • Canonical: P14941 (Residues: 1-164, 302-352; Coverage: 61%)
  • Canonical: P25984 (Residues: 165-301; Coverage: 39%)
Gene name: adh
Sequence domains: Alcohol dehydrogenase GroES-like domain
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 79.291Å b: 101.427Å c: 113.169Å
α: 90° β: 94.19° γ: 90°
R R work R free
0.164 0.161 0.22
Expression system: Escherichia coli