Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Pancreatic trypsin inhibitor Kunitz domain
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Pancreatic trypsin inhibitor Kunitz domain superfamily
- Peptidase S1, PA clan, chymotrypsin-like fold
- Proteinase inhibitor I2, Kunitz, conserved site
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
1 more domain
Structure domains:
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-133321 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease 1
Molecule details ›
Chain: E
Length: 223 amino acids
Theoretical weight: 23.33 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 223 amino acids
Theoretical weight: 23.33 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
- Canonical:
P00760 (Residues: 24-246; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Pancreatic trypsin inhibitor
Molecule details ›
Chain: I
Length: 58 amino acids
Theoretical weight: 6.51 KDa
Source organism: Bos taurus
Expression system: Escherichia coli HB101
UniProt:
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
Length: 58 amino acids
Theoretical weight: 6.51 KDa
Source organism: Bos taurus
Expression system: Escherichia coli HB101
UniProt:
- Canonical: P00974 (Residues: 36-93; Coverage: 73%)
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
