3fpc

X-ray diffraction
1.4Å resolution

Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH

Released:

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
Macromolecule:
NADP-dependent isopropanol dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 352 amino acids
Theoretical weight: 38.06 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P14941 (Residues: 1-162, 295-352; Coverage: 63%)
  • Canonical: P35630 (Residues: 163-294; Coverage: 37%)
Gene names: ADH1, adh
Sequence domains: Alcohol dehydrogenase GroES-like domain
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 79.742Å b: 82.429Å c: 118.249Å
α: 90° β: 99.89° γ: 90°
R-values:
R R work R free
0.118 0.116 0.155
Expression system: Escherichia coli