1g9a

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH AN INHIBITOR (EXPERIMENT 3)

Released:
Model geometry
Fit model/data
Data not deposited
Source organism: Clostridium botulinum
Primary publication:
A novel mechanism for Clostridium botulinum neurotoxin inhibition.
Biochemistry 41 9795-802 (2002)
PMID: 12146945

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-145485 (preferred)
Entry contents:
1 distinct polypeptide molecule

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 75.92Å b: 123.24Å c: 95.9Å
α: 90° β: 113.72° γ: 90°
R-values:
R R work R free
0.213 0.213 0.248