1e1h

X-ray diffraction
1.8Å resolution

Crystal Structure of recombinant Botulinum Neurotoxin Type A Light Chain, self-inhibiting Zn endopeptidase.

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:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
Non-polymer only tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Botulinum neurotoxin A2 light chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 287 amino acids
Theoretical weight: 32.15 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45894 (Residues: 5-250; Coverage: 19%)
Gene names: CLM_0897, atx, bna, bonT, botA
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Botulinum neurotoxin A2 light chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 174 amino acids
Theoretical weight: 20.56 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45894 (Residues: 251-416; Coverage: 13%)
Gene names: CLM_0897, atx, bna, bonT, botA
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 58.064Å b: 94.263Å c: 100.156Å
α: 90° β: 103.52° γ: 90°
R-values:
R R work R free
0.196 0.196 0.237
Expression system: Escherichia coli