3nf3

X-ray diffraction
2.4Å resolution

Crystal structure of BoNT/A LC with JTH-NB-7239 peptide

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163806 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
BoNT/A Chain: A
Molecule details ›
Chain: A
Length: 425 amino acids
Theoretical weight: 48.7 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7B8V4 (Residues: 1-420; Coverage: 32%)
Gene names: A, a, boNT, bont, bonta
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
JTH-NB72-39 inhibitor Chain: C
Molecule details ›
Chain: C
Length: 8 amino acids
Theoretical weight: 951 Da
Source organism: Clostridium botulinum
Expression system: Not provided

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21212
Unit cell:
a: 56.1Å b: 189.6Å c: 41.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.231
Expression systems:
  • Escherichia coli
  • Not provided