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 hexamer (preferred)
Assembly name:
Thrombin heavy chain and Glycocalicin (preferred)
PDBe Complex ID:
PDB-CPX-133153 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Glycocalicin
Molecule details ›
Chain: A
Length: 279 amino acids
Theoretical weight: 31.24 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
Sequence domains:
Structure domains: Ribonuclease Inhibitor
Length: 279 amino acids
Theoretical weight: 31.24 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
- Canonical:
P07359 (Residues: 17-294; Coverage: 44%)
Sequence domains:
Structure domains: Ribonuclease Inhibitor
Thrombin light chain
Molecule details ›
Chain: B
Length: 29 amino acids
Theoretical weight: 3.43 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Thrombin light chain
Length: 29 amino acids
Theoretical weight: 3.43 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P00734 (Residues: 333-361; Coverage: 5%)
Sequence domains: Thrombin light chain
Thrombin heavy chain
Molecule details ›
Chain: C
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: 364-621; Coverage: 43%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
