PDBe 3kuv

X-ray diffraction
1.5Å resolution

Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase FlK - T42S mutant in complex with acetate.

Released:

Function and Biology Details

Reaction catalysed:
Fluoroacetyl-CoA + H(2)O = fluoroacetate + CoA. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fluoroacetyl-CoA thioesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 139 amino acids
Theoretical weight: 15.27 KDa
Source organism: Streptomyces cattleya
Expression system: Escherichia coli
UniProt:
  • Canonical: Q1EMV2 (Residues: 1-139; Coverage: 100%)
Gene name: flK
Structure domains: Thiol Ester Dehydrase; Chain A

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2
Unit cell:
a: 62.296Å b: 92.678Å c: 49.109Å
α: 90° β: 100.61° γ: 90°
R-values:
R R work R free
0.195 0.181 0.219
Expression system: Escherichia coli