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:
- Fibrinogen, alpha/beta/gamma chain, coiled coil domain
- Prothrombin/thrombin
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Fibrinogen
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
3 more domains
Structure analysis Details
Assembly composition:
hetero decamer (preferred)
Assembly name:
Fibrinogen complex and Thrombin heavy chain (preferred)
PDBe Complex ID:
PDB-CPX-133150 (preferred)
Entry contents:
5 distinct polypeptide molecules
Macromolecules (5 distinct):
Thrombin light chain
Molecule details ›
Chains: A, D
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: B, E
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
Fibrinogen alpha chain
Molecule details ›
Chains: G, J
Length: 57 amino acids
Theoretical weight: 6.64 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Fibrinogen alpha/beta chain family
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 57 amino acids
Theoretical weight: 6.64 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P02671 (Residues: 36-92; Coverage: 7%)
Sequence domains: Fibrinogen alpha/beta chain family
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Fibrinogen beta chain
Molecule details ›
Chains: H, K
Length: 91 amino acids
Theoretical weight: 9.79 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Fibrinogen alpha/beta chain family
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 91 amino acids
Theoretical weight: 9.79 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P02675 (Residues: 45-135; Coverage: 20%)
Sequence domains: Fibrinogen alpha/beta chain family
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Fibrinogen gamma chain
Molecule details ›
Chains: I, L
Length: 45 amino acids
Theoretical weight: 5.1 KDa
Source organism: Homo sapiens
UniProt:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 45 amino acids
Theoretical weight: 5.1 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P02679 (Residues: 27-71; Coverage: 11%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
