Function and Biology Details
Reaction catalysed:
Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Prothrombin/thrombin
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Thrombin light chain
- Thrombin light chain domain superfamily
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
1 more domain
Structure domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Activation peptide fragment 2 (preferred)
PDBe Complex ID:
PDB-CPX-133163 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thrombin light chain
Molecule details ›
Chain: L
Length: 49 amino acids
Theoretical weight: 5.74 KDa
Source organism: Bos taurus
UniProt:
Sequence domains: Thrombin light chain
Length: 49 amino acids
Theoretical weight: 5.74 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P00735 (Residues: 318-366; Coverage: 8%)
Sequence domains: Thrombin light chain
Thrombin heavy chain
Molecule details ›
Chain: H
Length: 259 amino acids
Theoretical weight: 29.77 KDa
Source organism: Bos taurus
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 259 amino acids
Theoretical weight: 29.77 KDa
Source organism: Bos taurus
UniProt:
- Canonical: P00735 (Residues: 367-625; Coverage: 43%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
