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 |
Enzyme Information
| 3.4.22.16 |
Cathepsin H.
based on mapping to UniProt O46427
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.
-!- Present in lysosomes of mammalian cells. -!- Because of the combination of endopeptidase and aminopeptidase activity it can be considered as 'endoaminopeptidase'. -!- Belongs to peptidase family C1.
|
UniProtKB Entries (2)
| O46427 |
CATH_PIG
Sus scrofa
Pro-cathepsin H
|
| P01040 |
CYTA_HUMAN
Homo sapiens
Cystatin-A
|
PDB Structure
| PDB | 1NB3 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases
J.Mol.Biol.
|
