Function and Biology Details
Reactions catalysed:
Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
Degradation of blood coagulation factors Va and VIIIa.
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133069 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Thrombin light chain
Molecule details ›
Chains: A, C
Length: 32 amino acids
Theoretical weight: 3.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Thrombin light chain
Length: 32 amino acids
Theoretical weight: 3.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P00734 (Residues: 332-363; Coverage: 5%)
Sequence domains: Thrombin light chain
Thrombin heavy chain
Molecule details ›
Chains: B, D
Length: 259 amino acids
Theoretical weight: 29.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 259 amino acids
Theoretical weight: 29.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Activation peptide
Molecule details ›
Chains: E, F
Length: 20 amino acids
Theoretical weight: 2.32 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Length: 20 amino acids
Theoretical weight: 2.32 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: P04070 (Residues: 204-223; Coverage: 5%)
