PDBe 3kvi

X-ray diffraction
1.76Å resolution

Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase FlK - T42A mutant in complex with fluoro-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: 15.25 KDa
Source organism: Streptomyces cattleya
Expression system: Escherichia coli BL21(DE3)
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: SLS BEAMLINE X06DA
Spacegroup: C2
Unit cell:
a: 61.63Å b: 92.41Å c: 49.58Å
α: 90° β: 101.55° γ: 90°
R-values:
R R work R free
0.195 0.187 0.252
Expression system: Escherichia coli BL21(DE3)