CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.70 | Cathepsin D, subunit A; domain 1 |
|
2.40.70.10 | Acid Proteases |
Domain Context
CATH Clusters
| Superfamily | Acid Proteases |
| Functional Family | Vacuolar aspartic protease |
Enzyme Information
| 3.4.23.25 |
Saccharopepsin.
based on mapping to UniProt P07267
Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.
-!- Located in the vacuole. -!- Belongs to peptidase family A1. -!- Formerly EC 3.4.4.17, EC 3.4.23.6 and EC 3.4.23.8.
|
UniProtKB Entries (1)
| P07267 |
CARP_YEAST
Saccharomyces cerevisiae S288C
Saccharopepsin
|
PDB Structure
| PDB | 1DPJ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.
Nat.Struct.Biol.
|
