› 3rj9

X-ray diffraction
1.98Å resolution

Structure of alcohol dehydrogenase from Drosophila lebanonesis T114V mutant complexed with NAD+

Released:
DOI: 10.2210/pdb3rj9/pdb
PDB entry 3rj9 coloured by chain, front view.
PDB entry 3rj9 coloured by chain, side view.
PDB entry 3rj9 coloured by chain, top view.
Source organism: Scaptodrosophila lebanonensis
Primary publication:
An intact eight-membered water chain in drosophilid alcohol dehydrogenases is essential for optimal enzyme activity.
Wuxiuer Y, Morgunova E, Cols N, Popov A, Karshikoff A, Sylte I, Gonzàlez-Duarte R, Ladenstein R, Winberg JO
FEBS J 279 2940-56 (2012)
PMID: 22741949

Function and Biology Details

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

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, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 254 amino acids
Theoretical weight: 27.82 KDa
Source organism: Scaptodrosophila lebanonensis
Expression system: Escherichia coli
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 NAD 6 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 62.318Å b: 94.829Å c: 139.009Å
α: 90° β: 98.33° γ: 90°
R-values:
R R work R free
0.209 0.208 0.256
Expression system: Escherichia coli

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Citations

1 review citation

Rigidity versus flexibility: the dilemma of understanding protein thermal stability.
Karshikoff et al. (2015)
5 other articles