› 1adb

X-ray diffraction
2.4Å resolution

CRYSTALLOGRAPHIC STUDIES OF ISOSTERIC NAD ANALOGUES BOUND TO ALCOHOL DEHYDROGENASE: SPECIFICITY AND SUBSTRATE BINDING IN TWO TERNARY COMPLEXES

Released:
DOI: 10.2210/pdb1adb/pdb
PDB entry 1adb coloured by chain, front view.
PDB entry 1adb coloured by chain, side view.
PDB entry 1adb coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Crystallographic studies of isosteric NAD analogues bound to alcohol dehydrogenase: specificity and substrate binding in two ternary complexes.
Li H, Hallows WH, Punzi JS, Pankiewicz KW, Watanabe KA, Goldstein BM
Biochemistry 33 11734-44 (1994)
PMID: 7918390

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 Chains: A, B
Molecule details ›
Chains: A, B
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


Cofactor: Ligand CND 2 x CND
2 bound ligands:
Ligand ZN 4 x ZN
Ligand EOH 2 x EOH
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 52.1Å b: 44.7Å c: 93.5Å
α: 103.3° β: 87.9° γ: 70.4°
R-values:
R R work R free
0.18 0.18 not available
Expression system: Not provided

Quick links

Citations

6 review citations

The neurobiology of alcohol consumption and alcoholism: an integrative history.
Tabakoff et al. (2013)
5 more

7 mentions without citation

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