› 3jv7

X-ray diffraction
2Å resolution

Structure of ADH-A from Rhodococcus ruber

Released:
DOI: 10.2210/pdb3jv7/pdb
PDB entry 3jv7 coloured by chain, front view.
PDB entry 3jv7 coloured by chain, side view.
PDB entry 3jv7 coloured by chain, top view.
Source organism: Rhodococcus ruber
Primary publication:
Structural insights into substrate specificity and solvent tolerance in alcohol dehydrogenase ADH-'A' from Rhodococcus ruber DSM 44541.
Karabec M, Łyskowski A, Tauber KC, Steinkellner G, Kroutil W, Grogan G, Gruber K
Chem Commun (Camb) 46 6314-6 (2010)
PMID: 20676439

Function and Biology Details

Reaction catalysed: 
A primary alcohol + NAD(+) = an aldehyde + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185159 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
alcohol dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 345 amino acids
Theoretical weight: 35.22 KDa
Source organism: Rhodococcus ruber
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8KLT9 (Residues: 1-345; Coverage: 100%)
Gene names: RHRU231_470141, sadh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
3 bound ligands:
Ligand ZN 8 x ZN
Ligand ACY 4 x ACY
Ligand MPD 4 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21
Unit cell:
a: 65.822Å b: 106.119Å c: 109.097Å
α: 90° β: 91.26° γ: 90°
R-values:
R R work R free
0.162 0.159 0.206
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Preparation of pharmaceutical important fluorinated 1-arylethanols using isolated enzymes.
Hoff et al. (2013)
1 more

2 mentions without citation

Reversal of Regioselectivity in Zinc-Dependent Medium-Chain Alcohol Dehydrogenase from Rhodococcus erythropolis toward Octanone Derivatives.
Dhoke et al. (2020)
1 more