› 8adh

X-ray diffraction
2.4Å resolution

INTERDOMAIN MOTION IN LIVER ALCOHOL DEHYDROGENASE. STRUCTURAL AND ENERGETIC ANALYSIS OF THE HINGE BENDING MODE

Released:
DOI: 10.2210/pdb8adh/pdb
PDB entry 8adh coloured by chain, front view.
PDB entry 8adh coloured by chain, side view.
PDB entry 8adh coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Interdomain motion in liver alcohol dehydrogenase. Structural and energetic analysis of the hinge bending mode.
Colonna-Cesari F, Perahia D, Karplus M, Eklund H, Brädén CI, Tapia O
J Biol Chem 261 15273-80 (1986)
PMID: 3771574

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132405 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alcohol dehydrogenase E chain Chain: A
Molecule details ›
Chain: A
Length: 374 amino acids
Theoretical weight: 39.85 KDa
Source organism: Equus caballus
Expression system: Not provided
UniProt:
  • Canonical: P00327 (Residues: 2-375; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 56Å b: 75.2Å c: 181.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 not available not available
Expression system: Not provided

Quick links

Citations

5 review citations

Molecular characterization of microbial alcohol dehydrogenases.
Reid et al. (1994)
4 more

21 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
20 more