› 6sci

X-ray diffraction
1.95Å resolution

Structure of AdhE form 1

Released:
DOI: 10.2210/pdb6sci/pdb
PDB entry 6sci coloured by chain, front view.
PDB entry 6sci coloured by chain, side view.
PDB entry 6sci coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.
Azmi L, Bragginton EC, Cadby IT, Byron O, Roe AJ, Lovering AL, Gabrielsen M
Acta Crystallogr F Struct Biol Commun 76 414-421 (2020)
PMID: 32880589

Function and Biology Details

Reactions catalysed: 
A primary alcohol + NAD(+) = an aldehyde + NADH
Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141915 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional aldehyde-alcohol dehydrogenase AdhE Chains: A, B
Molecule details ›
Chains: A, B
Length: 455 amino acids
Theoretical weight: 49.9 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9Q7 (Residues: 451-891; Coverage: 50%)
Gene names: JW1228, adhE, ana, b1241
Sequence domains: Iron-containing alcohol dehydrogenase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 71.03Å b: 96.73Å c: 122.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.217
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics.
Zavarise et al. (2023)

1 mention without citation

High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.
Azmi et al. (2020)