Function and Biology Details
Reaction catalysed:
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proteinase inhibitor I13, potato inhibitor I
- Serine proteases, trypsin domain
- Peptidase S1A, chymotrypsin family
- Peptidase S1, PA clan, chymotrypsin-like fold
- Proteinase inhibitor I13, potato inhibitor I superfamily
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Chymotrypsin A chain C and Eglin C (preferred)
PDBe Complex ID:
PDB-CPX-133430 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chymotrypsinogen A
Molecule details ›
Chain: E
Length: 245 amino acids
Theoretical weight: 25.69 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 245 amino acids
Theoretical weight: 25.69 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
- Canonical:
P00766 (Residues: 1-245; Coverage: 100%)
Structure domains: Trypsin-like serine proteases
Eglin C
Molecule details ›
Chain: I
Length: 70 amino acids
Theoretical weight: 8.1 KDa
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
Structure domains: Trypsin Inhibitor V, subunit A
Length: 70 amino acids
Theoretical weight: 8.1 KDa
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
- Canonical: P01051 (Residues: 1-70; Coverage: 100%)
Structure domains: Trypsin Inhibitor V, subunit A
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
P21
Expression system: Not provided
