Function and Biology Details
Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185320 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase C1A papain C-terminal domain-containing protein
Molecule details ›
Chain: A
Length: 254 amino acids
Theoretical weight: 28.51 KDa
Source organism: Schistosoma mansoni
Expression system: Komagataella pastoris
UniProt:
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Length: 254 amino acids
Theoretical weight: 28.51 KDa
Source organism: Schistosoma mansoni
Expression system: Komagataella pastoris
UniProt:
- Canonical:
Q8MNY2 (Residues: 87-340; Coverage: 79%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
