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:
- Serine proteases, trypsin domain
- Prothrombin/thrombin
- Peptidase S1A, chymotrypsin family
- Peptidase S1, PA clan, chymotrypsin-like fold
- Staphylcoagulase, N-terminal, subdomain 2
- Staphylcoagulase, N-terminal, subdomain 1
- Staphylocoagulase, N-terminal, subdomain 1
- Serine proteases, trypsin family, serine active site
4 more domains
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133146 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thrombin heavy chain
Molecule details ›
Chains: A, D
Length: 291 amino acids
Theoretical weight: 33.47 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains:
Structure domains: Trypsin-like serine proteases
Length: 291 amino acids
Theoretical weight: 33.47 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P00734 (Residues: 332-622; Coverage: 49%)
Sequence domains:
Structure domains: Trypsin-like serine proteases
Staphylocoagulase N-terminal subdomain 1 domain-containing protein
Molecule details ›
Chains: C, F
Length: 281 amino acids
Theoretical weight: 33.21 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli BL21
UniProt:
Structure domains:
Length: 281 amino acids
Theoretical weight: 33.21 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli BL21
UniProt:
- Canonical: Q846V4 (Residues: 1-281; Coverage: 43%)
Structure domains:
