› 1geg

X-ray diffraction
1.7Å resolution

Function and Biology Details

Reaction catalysed: 
(S)-acetoin + NAD(+) = diacetyl + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175355 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diacetyl reductase [(S)-acetoin forming] Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 256 amino acids
Theoretical weight: 26.62 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q48436 (Residues: 1-256; Coverage: 100%)
Gene name: budC
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 8 x NAD
3 bound ligands:
Ligand GLC 8 x GLC
Ligand MG 4 x MG
Ligand BME 8 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL40B2
Spacegroup: P21
Unit cell:
a: 69.16Å b: 109.78Å c: 127.28Å
α: 90° β: 102.29° γ: 90°
R-values:
R R work R free
0.193 0.193 0.209
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structural insights into alcohol dehydrogenases catalyzing asymmetric reductions.
An et al. (2019)
16 other articles

15 mentions without citation

Mechanism of microbial production of acetoin and 2,3-butanediol optical isomers and substrate specificity of butanediol dehydrogenase.
Li et al. (2023)
14 more