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HIV-1 RT wild type and ADD: The best pose of ADD showed van der Waals interactions with RT residues Leu100, Val106, Val179, Tyr181, Tyr188, Val189 and Gly190, a hydrogen bond with Lys101 backbone (d = 2.21 Å) of its p66 subunit and van der Waals interactions with residues Glu138 and Thr139 of p51 subunit (Figure 3). ADD interacts out of the limits of NNIBP, where a significant part of the inhibitor is beyond the hydrophobic pocket, as delimited in the β-sheet (β6-β9-β10 and β12-β13-β14) by residues Tyr181, Tyr188 and Trp229 and above the entrance of the pocket (Pro95, Leu100, Lys101 and Lys103). This interaction mode is similar to delavirdine, which extends into the pocket, held by a hydrogen bond with residues in NNIBP. Herein, we can compare HDD and ADD to first generation NNRTIs, due to their similar conformation with TIBO and delavirdine, respectively [24].
Rt6 Software 2.21
2ff7e9595c
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