R-95845

R-95845 (α‑APA R‑95845) binds to the NNIBP of HIV-1 RT p66/p51 heterodimer in a butterfly-like conformation, inducing specific structural rearrangements in the enzyme and forming both hydrogen-bonding and hydrophobic interactions with surrounding residues, as characterized by a 2.8 Å resolution crystal structure with an R-factor of 25.5% and a free R-factor of 36.0%^[1].
R-95845 (α‑APA R‑95845) binds tightly to a hydrophobic pocket near the polymerase active site of purified HIV-1 p66/p51 RT, forming hydrogen bonds and aromatic interactions with specific p66 residues, and induces global and local conformational changes to the enzyme that likely underpin its inhibitory activity^[2].
R-95845 (α‑APA R‑95845) forms close contacts with group M HIV-1 subtype B BH10 RT via residues Tyr-181 and Val-179, as observed through crystal structure analysis^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.