Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
- not assigned
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, histidine active site
- Peptidase S1, PA clan
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Amyloid-beta protein 40/42 complex and Trypsin-3 (preferred)
PDBe Complex ID:
PDB-CPX-138360 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Trypsin-3
Molecule details ›
Chains: A, B
Length: 224 amino acids
Theoretical weight: 24.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli-Pichia pastoris shuttle vector pPpARG4
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 224 amino acids
Theoretical weight: 24.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli-Pichia pastoris shuttle vector pPpARG4
UniProt:
- Canonical:
P35030 (Residues: 81-304; Coverage: 74%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Soluble APP-beta
Molecule details ›
Chains: C, E
Length: 81 amino acids
Theoretical weight: 9.19 KDa
Source organism: Homo sapiens
Expression system: Komagataella phaffii GS115
UniProt:
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
Length: 81 amino acids
Theoretical weight: 9.19 KDa
Source organism: Homo sapiens
Expression system: Komagataella phaffii GS115
UniProt:
- Canonical: P05067 (Residues: 294-346; Coverage: 7%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
