4jra

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF THE BOTULINUM NEUROTOXIN A RECEPTOR-BINDING DOMAIN IN COMPLEX WITH THE LUMINAL DOMAIN Of SV2C

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 A heavy chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 443 amino acids
Theoretical weight: 51.72 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DPI1 (Residues: 871-1296; Coverage: 33%)
Gene names: CBO0806, CLC_0862, bna, botA
Sequence domains:
Structure domains:
Synaptic vesicle glycoprotein 2C Chains: C, D
Molecule details ›
Chains: C, D
Length: 136 amino acids
Theoretical weight: 15.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q496J9 (Residues: 456-574; Coverage: 16%)
Gene names: KIAA1054, SV2C
Sequence domains: Pentapeptide repeats (9 copies)
Structure domains: E3 ubiquitin-protein ligase SopA

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: C2
Unit cell:
a: 115.44Å b: 105.26Å c: 127.96Å
α: 90° β: 90.02° γ: 90°
R-values:
R R work R free
0.24 0.235 0.269
Expression system: Escherichia coli