› 1a72

X-ray diffraction
2.6Å resolution

AN ACTIVE-SITE DOUBLE MUTANT (PHE93->TRP, VAL203->ALA) OF HORSE LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH THE ISOSTERIC NAD ANALOG CPAD

Released:
DOI: 10.2210/pdb1a72/pdb
PDB entry 1a72 coloured by chain, front view.
PDB entry 1a72 coloured by chain, side view.
PDB entry 1a72 coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes.
Colby TD, Bahnson BJ, Chin JK, Klinman JP, Goldstein BM
Biochemistry 37 9295-304 (1998)
PMID: 9649310

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: 39.86 KDa
Source organism: Equus caballus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00327 (Residues: 2-375; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2221
Unit cell:
a: 55.5Å b: 74.2Å c: 179.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.3
Expression system: Escherichia coli

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Citations

9 review citations

Aldehyde dehydrogenase inhibitors: a comprehensive review of the pharmacology, mechanism of action, substrate specificity, and clinical application.
Koppaka et al. (2012)
8 more