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:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
alpha-thrombin complex and Hirudin variant-1 (preferred)
PDBe Complex ID:
PDB-CPX-133065 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Thrombin light chain
Molecule details ›
Chain: L
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: H
Length: 258 amino acids
Theoretical weight: 29.65 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 258 amino acids
Theoretical weight: 29.65 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P00734 (Residues: 364-621; Coverage: 43%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Hirudin variant-1
Molecule details ›
Chain: I
Length: 65 amino acids
Theoretical weight: 7.07 KDa
Source organism: Hirudo medicinalis
Expression system: Escherichia coli
UniProt:
Structure domains: Thrombin Inhibitor (Hirudin), subunit I
Length: 65 amino acids
Theoretical weight: 7.07 KDa
Source organism: Hirudo medicinalis
Expression system: Escherichia coli
UniProt:
- Canonical: P01050 (Residues: 3-65; Coverage: 97%)
Structure domains: Thrombin Inhibitor (Hirudin), subunit I
