2b83

X-ray diffraction
2.25Å resolution

A single amino acid substitution in the Clostridium beijerinckii alcohol dehydrogenase is critical for thermostabilization

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-150631 (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: 351 amino acids
Theoretical weight: 37.73 KDa
Source organism: Clostridium beijerinckii
Expression system: Escherichia coli
UniProt:
  • Canonical: P25984 (Residues: 1-351; Coverage: 100%)
Gene name: adh
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 79.47Å b: 103.34Å c: 193.307Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.193 0.23
Expression system: Escherichia coli