› 1b16

X-ray diffraction
1.4Å resolution

ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS TERNARY COMPLEX WITH NAD-3-PENTANONE

Released:
DOI: 10.2210/pdb1b16/pdb
PDB entry 1b16 coloured by chain, front view.
PDB entry 1b16 coloured by chain, side view.
PDB entry 1b16 coloured by chain, top view.
Source organism: Scaptodrosophila lebanonensis
Primary publication:
The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography.
Benach J, Atrian S, Gonzàlez-Duarte R, Ladenstein R
J Mol Biol 289 335-55 (1999)
PMID: 10366509

Function and Biology Details

Reaction catalysed: 
A primary alcohol + NAD(+) = an aldehyde + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145456 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alcohol dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 254 amino acids
Theoretical weight: 27.82 KDa
Source organism: Scaptodrosophila lebanonensis
UniProt:
  • Canonical: P10807 (Residues: 1-254; Coverage: 100%)
Gene name: Adh
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAQ 2 x NAQ
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P21
Unit cell:
a: 66.8Å b: 53Å c: 70.5Å
α: 90° β: 107.2° γ: 90°
R-values:
R R work R free
0.184 0.184 0.213

Quick links

Citations

6 review citations

Medium- and short-chain dehydrogenase/reductase gene and protein families : the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes.
Kavanagh et al. (2008)
5 more

5 mentions without citation

Recognition of functional sites in protein structures.
Shulman-Peleg et al. (2004)
4 more