Function and Biology Details
Reaction catalysed:
Specifically activates several components of the blood clotting system, including coagulation factor X, coagulation factor IX and protein C by cleavage of -Arg-|- bonds. Has no action on insulin B chain.
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
factor X-activating enzyme (preferred)
PDBe Complex ID:
PDB-CPX-175657 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (5 distinct):
Coagulation factor X-activating enzyme heavy chain
Molecule details ›
Chain: A
Length: 427 amino acids
Theoretical weight: 47.7 KDa
Source organism: Daboia siamensis
UniProt:
Structure domains: Collagenase (Catalytic Domain)
Length: 427 amino acids
Theoretical weight: 47.7 KDa
Source organism: Daboia siamensis
UniProt:
- Canonical:
Q7LZ61 (Residues: 189-615; Coverage: 71%)
Structure domains: Collagenase (Catalytic Domain)
Snaclec coagulation factor X-activating enzyme light chain 2
Molecule details ›
Chain: B
Length: 134 amino acids
Theoretical weight: 15.96 KDa
Source organism: Daboia siamensis
UniProt:
Sequence domains: Lectin C-type domain
Structure domains: Mannose-Binding Protein A, subunit A
Length: 134 amino acids
Theoretical weight: 15.96 KDa
Source organism: Daboia siamensis
UniProt:
- Canonical: Q4PRD2 (Residues: 25-158; Coverage: 100%)
Sequence domains: Lectin C-type domain
Structure domains: Mannose-Binding Protein A, subunit A
Snaclec coagulation factor X-activating enzyme light chain 1
Molecule details ›
Chain: C
Length: 122 amino acids
Theoretical weight: 14.36 KDa
Source organism: Daboia siamensis
UniProt:
Sequence domains: Lectin C-type domain
Structure domains: Mannose-Binding Protein A, subunit A
Length: 122 amino acids
Theoretical weight: 14.36 KDa
Source organism: Daboia siamensis
UniProt:
- Canonical: Q4PRD1 (Residues: 25-146; Coverage: 99%)
Sequence domains: Lectin C-type domain
Structure domains: Mannose-Binding Protein A, subunit A
