Literature summary for 3.4.23.16 extracted from

Chen, J.; Yang, M.; Hu, G.; Shi, S.; Yi, C.; Zhang, Q.
Insights into the functional role of protonation states in the HIV-1 protease-BEA369 complex: molecular dynamics simulations and free energy calculations (2009), J. Mol. Model., 15, 1245-1252.

Search for more literature for 3.4.23.16

Inhibitors

Inhibitors	Comment	Organism	Structure
BEA369	molecular dynamics simulation study on the role of protonation in the protease complex with inhibitor BEA369. Protonation of aspartic acids Asp25/Asp25' has a strong influence on the dynamics behavior of the complex, the binding free energy of BEA369, and inhibitor-residue interactions. Relative binding free energies show that protonation of Asp25 results in the strongest binding of BEA369 to HIV-1 protease. Inhibitor-residue interactions indicate that protonation of Asp25 has the most favorable effect on binding of BEA369. Protonation of Asp25 strongly influences the water-mediated link of a conserved water molecule, Wat301	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)