2vu9

X-ray diffraction
1.6Å resolution

CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN SEROTYPE A BINDING DOMAIN IN COMPLEX WITH GT1B

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
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Botulinum neurotoxin A heavy chain Chain: A
Molecule details ›
Chain: A
Length: 444 amino acids
Theoretical weight: 51.71 KDa
Source organism: Clostridium botulinum A
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0DPI1 (Residues: 874-1296; Coverage: 33%)
Gene names: CBO0806, CLC_0862, bna, botA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GAL, NGA, SIA
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: C2221
Unit cell:
a: 72.7Å b: 116.11Å c: 105.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.161 0.186
Expression system: Escherichia coli BL21