X-ray diffraction
2.2Å resolution

Crystal structure of crotonase from Clostridium acetobutylicum


Function and Biology Details

Reaction catalysed:
A short-chain (3S)-3-hydroxyacyl-CoA = a short-chain trans-2-enoyl-CoA + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Short-chain-enoyl-CoA hydratase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 267 amino acids
Theoretical weight: 29.05 KDa
Source organism: Clostridium acetobutylicum ATCC 824
Expression system: Escherichia coli
  • Canonical: P52046 (Residues: 1-261; Coverage: 100%)
Gene names: CA_C2712, crt
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P3212
Unit cell:
a: 78.673Å b: 78.673Å c: 210.703Å
α: 90° β: 90° γ: 120°
R R work R free
0.192 0.189 0.258
Expression system: Escherichia coli