Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-137566 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
von Willebrand factor
Molecule details ›
Chain: A
Length: 202 amino acids
Theoretical weight: 23.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: von Willebrand factor type A domain
Structure domains: von Willebrand factor, type A domain
Length: 202 amino acids
Theoretical weight: 23.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P04275 (Residues: 1263-1464; Coverage: 7%)
Sequence domains: von Willebrand factor type A domain
Structure domains: von Willebrand factor, type A domain
Snaclec botrocetin subunit alpha
Molecule details ›
Chain: B
Length: 133 amino acids
Theoretical weight: 15.23 KDa
Source organism: Bothrops jararaca
UniProt:
Structure domains: Mannose-Binding Protein A, subunit A
Length: 133 amino acids
Theoretical weight: 15.23 KDa
Source organism: Bothrops jararaca
UniProt:
- Canonical: P22029 (Residues: 1-133; Coverage: 100%)
Structure domains: Mannose-Binding Protein A, subunit A
Snaclec botrocetin subunit beta
Molecule details ›
Chain: C
Length: 125 amino acids
Theoretical weight: 15.05 KDa
Source organism: Bothrops jararaca
UniProt:
Structure domains: Mannose-Binding Protein A, subunit A
Length: 125 amino acids
Theoretical weight: 15.05 KDa
Source organism: Bothrops jararaca
UniProt:
- Canonical: P22030 (Residues: 1-125; Coverage: 100%)
Structure domains: Mannose-Binding Protein A, subunit A
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRL BEAMLINE BL11-1
Spacegroup:
P21
Expression system: Escherichia coli
