X-ray diffraction
1.58Å resolution

Leifsonia Alcohol Dehydrogenases LnADH


Function and Biology Details

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
Alcohol Dehydrogenases Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 251 amino acids
Theoretical weight: 25.26 KDa
Source organism: Leifsonia antarctica
Expression system: Escherichia coli

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NFPSS BEAMLINE BL19U1
Spacegroup: P21
Unit cell:
a: 54.671Å b: 238.522Å c: 68.921Å
α: 90° β: 113.35° γ: 90°
R R work R free
0.166 0.164 0.195
Expression system: Escherichia coli