Figure 4 | Scientific Reports

Figure 4

From: Deviated binding of anti-HBV nucleoside analog E-CFCP-TP to the reverse transcriptase active site attenuates the effect of drug-resistant mutations

Figure 4

Two distinct states (narrow and expanded state) of the hydrophobic pocket at the N-site in response to bound NAs/dNTP. Surface representation of the hydrophobic pocket with bound E-CFCP-TP in RT4M (expanded state) (a,d), ISL-TP in RTWT (expanded state) (b,e), and dGTP in RT4M (narrow state) (c,f). The views from two different directions are shown. The narrow and expanded states of the hydrophobic pocket are primarily due to the conformation of the Met184 sidechain. The residues creating the pocket, i.e., Ala114, Phe/Tyr115, Phe160, Met184, and Asp185, are colored green, orange, magenta, blue, and red, respectively. The schematic representations of the extended and narrow states of the hydrophobic pocket are also shown in (g–i). The close contact area is highlighted in light pink.

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