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:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thrombin light chain
Molecule details ›
Chain: A
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
- Canonical:
P00734 (Residues: 328-363; Coverage: 6%)
Thrombin heavy chain
Molecule details ›
Chain: B
Length: 259 amino acids
Theoretical weight: 29.71 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 259 amino acids
Theoretical weight: 29.71 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
- Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Structure domains: Trypsin-like serine proteases
