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 proteinase |
Enzyme Information
| 3.4.23.40 |
Phytepsin.
based on mapping to UniProt P42210
Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds.
-!- Known particularly fron barley grain, but present in other plants also. -!- Belongs to peptidase family A1.
|
UniProtKB Entries (1)
| P42210 |
ASPR_HORVU
Hordeum vulgare
Phytepsin
|
PDB Structure
| PDB | 1QDM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.
EMBO J.
|