Function and Biology Details
Reaction catalysed:
Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Pancreatic trypsin inhibitor Kunitz domain
- Serine proteases, trypsin domain
- Peptidase S1A, chymotrypsin family
- Pancreatic trypsin inhibitor Kunitz domain superfamily
- Proteinase inhibitor I2, Kunitz, conserved site
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan, chymotrypsin-like fold
1 more domain
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133235 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Plasmin light chain B
Molecule details ›
Chains: A, B
Length: 247 amino acids
Theoretical weight: 27.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 247 amino acids
Theoretical weight: 27.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P00747 (Residues: 564-810; Coverage: 31%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Kunitz-type serine protease inhibitor textilinin-1
Molecule details ›
Chains: C, D
Length: 59 amino acids
Theoretical weight: 6.7 KDa
Source organism: Pseudonaja textilis textilis
Expression system: Escherichia coli
UniProt:
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
Length: 59 amino acids
Theoretical weight: 6.7 KDa
Source organism: Pseudonaja textilis textilis
Expression system: Escherichia coli
UniProt:
- Canonical: Q90WA1 (Residues: 25-83; Coverage: 100%)
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
