Structure analysis

THE CRYSTAL STRUCTURE OF EXOENZYME C3 FROM CLOSTRIDIUM BOTULINUM

X-ray diffraction
1.7Å resolution
Source organism: Clostridium botulinum
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 10922.42 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-147514
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 10884.29 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-147514
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 11014.21 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-147514
Assembly 4
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Multimeric state: monomeric
Accessible surface area: 10875.9 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-147514

Macromolecules

Chains: A, B, C, D
Length: 211 amino acids
Theoretical weight: 23.59 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: P15879 (Residues: 41-251; Coverage: 100%)
Gene name: C3
Pfam: ADP-ribosyltransferase exoenzyme
InterPro:
CATH: Toxin ADP-ribosyltransferase; Chain A, domain 1
SCOP: ADP-ribosylating toxins

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