Function and Biology Details
Reaction catalysed:
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
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
- 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-133428 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chymotrypsinogen A
Molecule details ›
Chains: A, C
Length: 245 amino acids
Theoretical weight: 25.69 KDa
Source organism: Bos taurus
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 245 amino acids
Theoretical weight: 25.69 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P00766 (Residues: 1-245; Coverage: 100%)
Structure domains: Trypsin-like serine proteases
Pancreatic trypsin inhibitor
Molecule details ›
Chains: B, D
Length: 58 amino acids
Theoretical weight: 6.48 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
Length: 58 amino acids
Theoretical weight: 6.48 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P00974 (Residues: 36-93; Coverage: 73%)
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
