PDBe 3fii

X-ray diffraction
2.17Å resolution

Crystal structure of Clostridium botulinum neurotoxin serotype F catalytic domain with an inhibitor (inh2)

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Botulinum neurotoxin F light chain Chain: A
Molecule details ›
Chain: A
Length: 427 amino acids
Theoretical weight: 48.75 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: A7GBG3 (Residues: 1-419; Coverage: 33%)
Gene names: CLI_0851, F, boNT/F, bont
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Vesicle-associated membrane protein 2 Chain: B
Molecule details ›
Chain: B
Length: 33 amino acids
Theoretical weight: 3.81 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P63027 (Residues: 27-57; Coverage: 27%)
Gene names: SYB2, VAMP2

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 55.592Å b: 70.353Å c: 113.929Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.246 0.246 0.29
Expression systems:
  • Escherichia coli
  • Not provided