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:
- Prothrombin/thrombin
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- 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 analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106843 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Putative secreted salivary protein
Molecule details ›
Chains: A, N, O, P, Q, R
Length: 36 amino acids
Theoretical weight: 3.87 KDa
Source organism: Xenopsylla cheopis
Expression system: Not provided
UniProt:
Length: 36 amino acids
Theoretical weight: 3.87 KDa
Source organism: Xenopsylla cheopis
Expression system: Not provided
UniProt:
- Canonical:
A2IAB2 (Residues: 24-59; Coverage: 100%)
Thrombin light chain
Molecule details ›
Chains: B, D, F, I, K, L
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 ›
Chains: C, E, G, H, J, M
Length: 259 amino acids
Theoretical weight: 29.78 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Trypsin
Length: 259 amino acids
Theoretical weight: 29.78 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Sequence domains: Trypsin
