3ddb

X-ray diffraction
1.6Å resolution

Crystal structure of the catalytic domain of Botulinum neurotoxin serotype a with a substrate analog 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)
PDBe Complex ID:
PDB-CPX-144073 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Botulinum neurotoxin A light chain Chain: A
Molecule details ›
Chain: A
Length: 430 amino acids
Theoretical weight: 49.42 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DPI1 (Residues: 1-424; Coverage: 33%)
Gene names: CBO0806, CLC_0862, bna, botA
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Synaptosomal-associated protein 25 Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 763 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P60880 (Residues: 197-202; Coverage: 3%)
Gene names: SNAP, SNAP25

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 50.871Å b: 66.581Å c: 65.062Å
α: 90° β: 98.34° γ: 90°
R-values:
R R work R free
0.2 0.2 0.218
Expression systems:
  • Escherichia coli
  • Not provided