CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.70 | Cathepsin B; Chain A |
|
3.90.70.10 | Cysteine proteinases |
Domain Context
CATH Clusters
| Superfamily | Cysteine proteinases |
| Functional Family | Cathepsin B |
Enzyme Information
| 3.4.22.1 |
Cathepsin B.
based on mapping to UniProt P07858
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.
-!- An intracellular (lysosomal) enzyme. -!- Belongs to peptidase family C1.
|
UniProtKB Entries (2)
| Q966X9 |
CHAG_TRYCR
Trypanosoma cruzi
Chagasin
|
| P07858 |
CATB_HUMAN
Homo sapiens
Cathepsin B
|
PDB Structure
| PDB | 3CBK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Displacement of the occluding loop by the parasite protein, chagasin, results in efficient inhibition of human cathepsin B.
J.Biol.Chem.
|