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
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
- Thrombin light chain domain superfamily
1 more domain
Structure analysis Details
Assemblies composition:
Assembly name:
Thrombin light chain (preferred)
PDBe Complex ID:
PDB-CPX-148522 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Thrombin light chain
Molecule details ›
Chain: A
Length: 42 amino acids
Theoretical weight: 4.82 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
Sequence domains: Thrombin light chain
Length: 42 amino acids
Theoretical weight: 4.82 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
- Canonical:
P19221 (Residues: 319-360; Coverage: 7%)
Sequence domains: Thrombin light chain
Thrombin heavy chain
Molecule details ›
Chain: B
Length: 259 amino acids
Theoretical weight: 30.01 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 259 amino acids
Theoretical weight: 30.01 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
- Canonical: P19221 (Residues: 361-618; Coverage: 43%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
