3a28

X-ray diffraction
2Å resolution

Crystal structure of L-2,3-butanediol dehydrogenase

Released:

Function and Biology Details

Reactions catalysed:
(S)-acetoin + NAD(+) = diacetyl + NADH
(2S,3S)-butane-2,3-diol + NAD(+) = (S)-acetoin + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-2,3-butanediol dehydrogenase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 258 amino acids
Theoretical weight: 27.13 KDa
Source organism: Corynebacterium glutamicum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZNN8 (Residues: 1-258; Coverage: 100%)
Gene name: budC
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 8 x NAD
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P1
Unit cell:
a: 60.8Å b: 69.2Å c: 127.4Å
α: 96.1° β: 100.2° γ: 109.6°
R-values:
R R work R free
0.193 0.193 0.24
Expression system: Escherichia coli