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 | Aspartic protease |
Enzyme Information
| 3.4.23.24 |
Candidapepsin.
based on mapping to UniProt P0CS83
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.
-!- This endopeptidase from the imperfect yeast Candida albicans is inhibited by pepstatin, but not by methyl 2-diazoacetamido-hexanoate or 1,2-epoxy-3-(p-nitrophenoxy)propane. -!- Belongs to peptidase family A1. -!- Formerly EC 3.4.4.17 and EC 3.4.23.6.
|
UniProtKB Entries (1)
| P0CS83 |
CARP2_CANAX
Candida albicans
Candidapepsin-2
|
PDB Structure
| PDB | 3PVK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Experimental and computational active site mapping as a starting point to fragment-based lead discovery.
Chemmedchem
|