› 4bt3

X-ray diffraction
1.1Å resolution

acetolactate decarboxylase with a bound (2R,3R)-2,3-Dihydroxy-2- methylbutanoic acid

Released:
DOI: 10.2210/pdb4bt3/pdb
PDB entry 4bt3 coloured by chain, front view.
PDB entry 4bt3 coloured by chain, side view.
PDB entry 4bt3 coloured by chain, top view.
Source organism: Brevibacillus brevis
Primary publication:
Structure and mechanism of acetolactate decarboxylase.
Marlow VA, Rea D, Najmudin S, Wills M, Fülöp V
ACS Chem Biol 8 2339-44 (2013)
PMID: 23985082

Function and Biology Details

Reaction catalysed: 
(2S)-2-hydroxy-2-methyl-3-oxobutanoate = (3R)-3-hydroxybutan-2-one + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150028 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-acetolactate decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 257 amino acids
Theoretical weight: 28.83 KDa
Source organism: Brevibacillus brevis
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P23616 (Residues: 29-285; Coverage: 99%)
Gene name: aldB
Sequence domains: Alpha-acetolactate decarboxylase
Structure domains: Hypothetical protein, similar to alpha- acetolactate decarboxylase; domain 2

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand WTZ 1 x WTZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P3221
Unit cell:
a: 47.11Å b: 47.11Å c: 198.91Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.207 0.225
Expression system: Bacillus subtilis

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Citations

5 citation in other articles

Reconstruction of an acetogenic 2,3-butanediol pathway involving a novel NADPH-dependent primary-secondary alcohol dehydrogenase.
Köpke et al. (2014)
4 more