Function and Biology Details
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175081 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Hemagglutinin component HA-70 C-terminal domain-containing protein
Molecule details ›
Chains: A, C, E, G
Length: 254 amino acids
Theoretical weight: 28.85 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
Sequence domains: Haemagglutinin 70 C-terminal domain
Structure domains: Jelly Rolls
Length: 254 amino acids
Theoretical weight: 28.85 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8KHU9 (Residues: 378-626; Coverage: 40%)
Sequence domains: Haemagglutinin 70 C-terminal domain
Structure domains: Jelly Rolls
HA-17
Molecule details ›
Chains: B, D, F, H
Length: 147 amino acids
Theoretical weight: 17.07 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
Sequence domains: Clostridium botulinum HA-17 domain
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Length: 147 amino acids
Theoretical weight: 17.07 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
- Canonical: Q45878 (Residues: 2-146; Coverage: 99%)
Sequence domains: Clostridium botulinum HA-17 domain
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 24-ID-C
Spacegroup:
P21
Expression system: Escherichia coli
