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 variant-1 (preferred)
PDBe Complex ID:
PDB-CPX-133139 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thrombin heavy chain
Molecule details ›
Chain: A
Length: 288 amino acids
Theoretical weight: 33.15 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains:
Structure domains: Trypsin-like serine proteases
Length: 288 amino acids
Theoretical weight: 33.15 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P00734 (Residues: 334-621; Coverage: 48%)
Sequence domains:
Structure domains: Trypsin-like serine proteases
Hirudin variant-1
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: P01050 (Residues: 55-64; Coverage: 15%)
