CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.5 | Single alpha-helices involved in coiled-coils or other helix-helix interfaces |
|
1.20.5.170 |
Domain Context
CATH Clusters
| Superfamily | 1.20.5.170 |
| Functional Family |
Enzyme Information
| 3.4.22.1 |
Cathepsin B.
based on mapping to UniProt P07688
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)
| P07688 |
CATB_BOVIN
Bos taurus
Cathepsin B
|
PDB Structure
| PDB | 1SP4 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of NS-134 in complex with bovine cathepsin B: a two-headed epoxysuccinyl inhibitor extends along the entire active-site cleft.
Biochem.J.
|