Function and Biology Details
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175079 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ricin B lectin domain-containing protein
Molecule details ›
Chains: A, B
Length: 296 amino acids
Theoretical weight: 34.08 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
Sequence domains: Ricin-type beta-trefoil lectin domain-like
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Length: 296 amino acids
Theoretical weight: 34.08 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
- Canonical:
Q45871 (Residues: 2-293; Coverage: 100%)
Sequence domains: Ricin-type beta-trefoil lectin domain-like
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)
HA-17
Molecule details ›
Chain: C
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:
C2221
Expression system: Escherichia coli
