X-ray diffraction
2.3Å resolution

Crystal structure of thiolase mutation (V77Q,N153Y,A286K) from Clostridium acetobutylicum


Function and Biology Details

Reaction catalysed:
(1a) acetyl-CoA + [acetyl-CoA C-acetyltransferase]-L-cysteine = [acetyl-CoA C-acetyltransferase]-S-acetyl-L-cysteine + CoA
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Acetyl-CoA acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 400 amino acids
Theoretical weight: 42.5 KDa
Source organism: Clostridium acetobutylicum ATCC 824
Expression system: Escherichia coli
  • Canonical: P45359 (Residues: 1-392; Coverage: 100%)
Gene names: CA_C2873, thl, thlA
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: C2
Unit cell:
a: 116.434Å b: 131.201Å c: 54.12Å
α: 90° β: 110.3° γ: 90°
R R work R free
0.154 0.151 0.213
Expression system: Escherichia coli