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Literature summary for 2.5.1.96 extracted from
- Molecular docking studies to map the binding site of squalene synthase inhibitors on dehydrosqualene synthase of Staphylococcus aureus (2010), J. Biomol. Struct. Dyn., 28, 201-210.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| docking analysis of lapaquistat acetate and squalestatin to crtM. Residues H18, R45, D48, D52, Y129, Q165, N168 and D172 interact with the inhibitors | Staphylococcus aureus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| lapaquistat acetate | docking analysis, interaction with residues H18, R45, D48, D52, Y129, Q165, N168 and D172 | Staphylococcus aureus |  |
| squalestatin | docking analysis, interaction with residues H18, R45, D48, D52, Y129, Q165, N168 and D172 | Staphylococcus aureus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | - |
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Release 2023.1 (January 2023)
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