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:
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Prothrombin/thrombin
- Peptidase S1A, chymotrypsin family
- Peptidase S1, PA clan
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Thrombin light chain domain superfamily
1 more domain
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
alpha-thrombin complex and Hirudin-2 (preferred)
PDBe Complex ID:
PDB-CPX-133058 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Thrombin light chain
Molecule details ›
Chain: A
Length: 27 amino acids
Theoretical weight: 3.19 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Thrombin light chain
Length: 27 amino acids
Theoretical weight: 3.19 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P00734 (Residues: 334-360; Coverage: 5%)
Sequence domains: Thrombin light chain
Thrombin heavy chain
Molecule details ›
Chain: B
Length: 147 amino acids
Theoretical weight: 17.07 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 147 amino acids
Theoretical weight: 17.07 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P00734 (Residues: 364-510; Coverage: 25%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Thrombin heavy chain
Hirudin-2
