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:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Chagasin and Cathepsin B heavy chain (preferred)
PDBe Complex ID:
PDB-CPX-139799 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin B
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 29.31 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Length: 266 amino acids
Theoretical weight: 29.31 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
- Canonical:
P07858 (Residues: 74-339; Coverage: 83%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Chagasin
Molecule details ›
Chain: B
Length: 110 amino acids
Theoretical weight: 12.05 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
Sequence domains: Chagasin family peptidase inhibitor I42
Structure domains: Immunoglobulin-like
Length: 110 amino acids
Theoretical weight: 12.05 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
- Canonical: Q966X9 (Residues: 1-110; Coverage: 100%)
Sequence domains: Chagasin family peptidase inhibitor I42
Structure domains: Immunoglobulin-like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
MAX II BEAMLINE I911-2
Spacegroup:
P42212
Expression systems:
- Komagataella pastoris
- Escherichia coli
