Function and Biology Details
Reaction catalysed:
Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assemblies composition:
PDBe Complex ID:
PDB-CPX-133222 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Snaclec agkisacutacin subunit A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.68 KDa
Source organism: Deinagkistrodon acutus
UniProt:
Structure domains: Mannose-Binding Protein A, subunit A
Length: 129 amino acids
Theoretical weight: 14.68 KDa
Source organism: Deinagkistrodon acutus
UniProt:
- Canonical:
Q9IAM1 (Residues: 24-152; Coverage: 100%)
Structure domains: Mannose-Binding Protein A, subunit A
Snaclec anticoagulant protein subunit B
Molecule details ›
Chain: B
Length: 123 amino acids
Theoretical weight: 14.58 KDa
Source organism: Deinagkistrodon acutus
UniProt:
Structure domains: Mannose-Binding Protein A, subunit A
Length: 123 amino acids
Theoretical weight: 14.58 KDa
Source organism: Deinagkistrodon acutus
UniProt:
- Canonical: Q9DEF8 (Residues: 24-146; Coverage: 100%)
Structure domains: Mannose-Binding Protein A, subunit A
Factor X light chain
Molecule details ›
Chain: G
Length: 44 amino acids
Theoretical weight: 5.73 KDa
Source organism: Bos taurus
UniProt:
Sequence domains: Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain
Length: 44 amino acids
Theoretical weight: 5.73 KDa
Source organism: Bos taurus
UniProt:
- Canonical: P00743 (Residues: 41-84; Coverage: 9%)
Sequence domains: Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain
