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 P00787
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 (1)
| P00787 |
CATB_RAT
Rattus norvegicus
Cathepsin B
|
PDB Structure
| PDB | 1THE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Saccharomyces |
| Primary Citation |
Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design.
J.Biol.Chem.
|
