› 5o8q

X-ray diffraction
2.22Å resolution

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alcohol dehydrogenase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 352 amino acids
Theoretical weight: 35.97 KDa
Source organism: Rhodococcus sp. M8
Expression system: Escherichia coli BL21
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 16 x ZN
Ligand NAD 8 x NAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 103.689Å b: 109.458Å c: 256.653Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.194 0.216
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

A mechanistic view of enzyme evolution.
Yang et al. (2020)
1 more

1 mention without citation

Relaxation of nonproductive binding and increased rate of coenzyme release in an alcohol dehydrogenase increases turnover with a nonpreferred alcohol enantiomer.
Hamnevik et al. (2017)