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:
Structure domains:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
alpha-thrombin complex and Glycocalicin (preferred)
PDBe Complex ID:
PDB-CPX-133074 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (5 distinct):
Thrombin light chain
Molecule details ›
Chain: A
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Thrombin light chain
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P00734 (Residues: 328-363; Coverage: 6%)
Sequence domains: Thrombin light chain
Thrombin heavy chain
Molecule details ›
Chain: B
Length: 259 amino acids
Theoretical weight: 29.78 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 259 amino acids
Theoretical weight: 29.78 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Glycocalicin
Molecule details ›
Chain: G
Length: 290 amino acids
Theoretical weight: 32.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Ribonuclease Inhibitor
Length: 290 amino acids
Theoretical weight: 32.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P07359 (Residues: 17-306; Coverage: 46%)
Sequence domains:
Structure domains: Ribonuclease Inhibitor
