Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | study the potentially important structural differences in active sites of both proteins responsible for making the inhibitors selective for Escherichia coli as compared to Pseudomonas aeruginosa LpxC, homology models of the LpxC of both organisms are developed and validated on the basis of a 3D profile and PROCHECK. Subsequently, a molecular electrostatic potential (MEP)-based surface and cavity-depth analysis is performed. Finally, a cross-docking analysis of reported inhibitors is performed to reveal selective binding modes. These studies identify differences between the two active sites and have implications for designing effective strategies to identify LpxC inhibitors that can be developed as novel broad-spectrum antibacterial drugs | Escherichia coli | |
additional information | study the potentially important structural differences in active sites of both proteins responsible for making the inhibitors selective for Escherichia coli as compared to Pseudomonas aeruginosa LpxC, homology models of the LpxC of both organisms are developed and validated on the basis of a 3D profile and PROCHECK. Subsequently, a molecular electrostatic potential (MEP)-based surface and cavity-depth analysis is performed. Finally, a cross-docking analysis of reported inhibitors is performed to reveal selective binding modes. These studies identify differences between the two active sites and have implications for designing effective strategies to identify LpxC inhibitors that can be developed as novel broad-spectrum antibacterial drugs | Pseudomonas aeruginosa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Pseudomonas aeruginosa | P47205 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
deacetylase LpxC | - |
Escherichia coli |
deacetylase LpxC | - |
Pseudomonas aeruginosa |