CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.10 | Ribbon |
|
2.10.55 | Leishmanolysin; domain 3 |
|
2.10.55.10 | Leishmanolysin domain 3 |
Domain Context
CATH Clusters
| Superfamily | Leishmanolysin domain 3 |
| Functional Family | MSP-A1 surface protease homolog |
Enzyme Information
| 3.4.24.36 |
Leishmanolysin.
based on mapping to UniProt P08148
Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.
-!- A membrane-bound glycoprotein found on the promastigote of various species of Leishmania protozoans. -!- Contains consensus sequence for a zinc binding site; Z-Tyr-Leu-NHOH is a strong inhibitor. -!- The enzyme can activate its proenzyme by cleavage of the 100- Val-|-Val-101 bond. -!- An acidic pH optimum is found with certain protein substrates. -!- Belongs to peptidase family M8.
|
UniProtKB Entries (1)
| P08148 |
GP63_LEIMA
Leishmania major
Leishmanolysin
|
PDB Structure
| PDB | 1LML |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63).
Structure
|
