2a97

X-ray diffraction
1.8Å resolution

Crystal structure of catalytic domain of Clostridium botulinum neurotoxin serotype F

Released:

Function and Biology Details

Reaction catalysed:
Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or syntaxin. No detected action on small molecule substrates.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-151870 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Botulinum neurotoxin F light chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 439 amino acids
Theoretical weight: 49.96 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30996 (Residues: 1-439; Coverage: 35%)
Gene name: botF
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: C2
Unit cell:
a: 173.4Å b: 53.24Å c: 113.87Å
α: 90° β: 119.17° γ: 90°
R-values:
R R work R free
0.241 0.241 0.269
Expression system: Escherichia coli BL21(DE3)