5jmc

X-ray diffraction
2.64Å resolution

Receptor binding domain of Botulinum neurotoxin A in complex with rat 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, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 433 amino acids
Theoretical weight: 50.47 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DPI1 (Residues: 872-1296; Coverage: 33%)
Gene names: CBO0806, CLC_0862, bna, botA
Sequence domains:
Structure domains:
Synaptic vesicle glycoprotein 2C Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 124 amino acids
Theoretical weight: 14.52 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Z2I6 (Residues: 455-577; Coverage: 17%)
Gene name: Sv2c
Sequence domains: Pentapeptide repeats (9 copies)
Structure domains: E3 ubiquitin-protein ligase SopA

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 88.662Å b: 143.989Å c: 110.917Å
α: 90° β: 93.62° γ: 90°
R-values:
R R work R free
0.241 0.24 0.275
Expression system: Escherichia coli