Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-137569 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Snaclec bitiscetin subunit alpha
Molecule details ›
Chain: A
Length: 131 amino acids
Theoretical weight: 14.95 KDa
Source organism: Bitis arietans
UniProt:
Structure domains: Mannose-Binding Protein A, subunit A
Length: 131 amino acids
Theoretical weight: 14.95 KDa
Source organism: Bitis arietans
UniProt:
- Canonical:
Q7LZK5 (Residues: 1-131; Coverage: 100%)
Structure domains: Mannose-Binding Protein A, subunit A
Snaclec bitiscetin subunit beta
Molecule details ›
Chain: B
Length: 125 amino acids
Theoretical weight: 14.82 KDa
Source organism: Bitis arietans
UniProt:
Structure domains: Mannose-Binding Protein A, subunit A
Length: 125 amino acids
Theoretical weight: 14.82 KDa
Source organism: Bitis arietans
UniProt:
- Canonical: Q7LZK8 (Residues: 1-125; Coverage: 100%)
Structure domains: Mannose-Binding Protein A, subunit A
von Willebrand factor
Molecule details ›
Chain: C
Length: 209 amino acids
Theoretical weight: 23.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: von Willebrand factor type A domain
Structure domains: von Willebrand factor, type A domain
Length: 209 amino acids
Theoretical weight: 23.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P04275 (Residues: 1260-1468; Coverage: 8%)
Sequence domains: von Willebrand factor type A domain
Structure domains: von Willebrand factor, type A domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE BL-6B
Spacegroup:
P43
Expression system: Escherichia coli BL21(DE3)
