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 domain:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
alpha-thrombin complex and peptide (preferred)
PDBe Complex ID:
PDB-CPX-133096 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Thrombin light chain
Molecule details ›
Chain: A
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
Sequence domains: Thrombin light chain
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
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: 29.73 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 259 amino acids
Theoretical weight: 29.73 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
- Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 19-ID
Spacegroup:
P212121
Expression system: Saccharomyces cerevisiae
