› 6acq

X-ray diffraction
2.5Å resolution

Crystal structure of (S)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium acetobutylicum, apo form

Released:
DOI: 10.2210/pdb6acq/pdb
PDB entry 6acq coloured by chain, front view.
PDB entry 6acq coloured by chain, side view.
PDB entry 6acq coloured by chain, top view.
Source organism: Clostridium acetobutylicum ATCC 824
Primary publication:
Crystal structure and kinetic analyses of a hexameric form of (S)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium acetobutylicum.
Takenoya M, Taguchi S, Yajima S
Acta Crystallogr F Struct Biol Commun 74 733-740 (2018)
PMID: 30387779

Function and Biology Details

Reaction catalysed: 
(S)-3-hydroxybutanoyl-CoA + NADP(+) = 3-acetoacetyl-CoA + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156457 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-hydroxybutyryl-CoA dehydrogenase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 302 amino acids
Theoretical weight: 32.79 KDa
Source organism: Clostridium acetobutylicum ATCC 824
Expression system: Escherichia coli
UniProt:
  • Canonical: P52041 (Residues: 1-282; Coverage: 100%)
Gene names: CA_C2708, hbd
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P212121
Unit cell:
a: 133.434Å b: 134.479Å c: 153.804Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.199 0.222
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

A (S)-3-Hydroxybutyrate Dehydrogenase Belonging to the 3-Hydroxyacyl-CoA Dehydrogenase Family Facilitates Hydroxyacid Degradation in Anaerobic Bacteria.
Zhou et al. (2023)
1 more

3 mentions without citation

Crystal structure and kinetic analyses of a hexameric form of (S)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium acetobutylicum.
Takenoya et al. (2018)
2 more