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
- Prothrombin/thrombin
- Peptidase S1A, chymotrypsin family
- 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 domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
alpha-thrombin complex and Hirudin-2' (preferred)
PDBe Complex ID:
PDB-CPX-133141 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thrombin heavy chain
Molecule details ›
Chain: E
Length: 295 amino acids
Theoretical weight: 33.86 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Sequence domains:
Structure domains: Trypsin-like serine proteases
Length: 295 amino acids
Theoretical weight: 33.86 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical:
P00734 (Residues: 328-622; Coverage: 49%)
Sequence domains:
Structure domains: Trypsin-like serine proteases
Hirudin-2'
Molecule details ›
Chain: I
Length: 10 amino acids
Theoretical weight: 1.36 KDa
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
Length: 10 amino acids
Theoretical weight: 1.36 KDa
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
- Canonical: P28505 (Residues: 55-64; Coverage: 15%)
