› 5vn1

X-ray diffraction
1.25Å resolution

horse liver alcohol dehydrogenae complexed with NADH (R,S)-N-1-methylhexylformamide

Released:
DOI: 10.2210/pdb5vn1/pdb
PDB entry 5vn1 coloured by chain, front view.
PDB entry 5vn1 coloured by chain, side view.
PDB entry 5vn1 coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis.
Plapp BV, Savarimuthu BR, Ferraro DJ, Rubach JK, Brown EN, Ramaswamy S
OpenAccess logo Biochemistry 56 3632-3646 (2017)
PMID: 28640600

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-523416 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alcohol dehydrogenase E chain Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 374 amino acids
Theoretical weight: 39.85 KDa
Source organism: Equus caballus
UniProt:
  • Canonical: P00327 (Residues: 2-375; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAI 4 x NAI
4 bound ligands:
Ligand ZN 8 x ZN
Ligand NWH 4 x NWH
Ligand MRD 2 x MRD
Ligand NMH 1 x NMH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 50.212Å b: 180.808Å c: 86.841Å
α: 90° β: 106.12° γ: 90°
R-values:
R R work R free
0.152 0.152 0.187

Quick links

Citations

8 citation in other articles

Expansion of the Catalytic Repertoire of Alcohol Dehydrogenases in Plant Metabolism.
Langley et al. (2022)
7 more

3 mentions without citation

Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis.
Plapp et al. (2017)
2 more