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Figure 4.
Figure 4. Close-up of the non-nucleoside inhibitor-binding
pocket in the structure of the HIV-1 RT/α-APA complex looking
through a putative entrance to the pocket, showing interactions
between α-APA and nearby amino acid residues. α-APA is shown
in purple as a ball-and-stick model with carbons purple,
nitrogens cyan, oxygens red and bromines magenta. The β7–β8
portion of p51 has a dashed outline. The side chains are shown
for the amino acid residues that make close contacts with α-APA
(in green), and for the three essential aspartic acid residues
D110, D185 and D186 (in red) at the polymerase active site.
Dashed lines indicate connections between the side chains and
the β-strands. Figure 4. Close-up of the non-nucleoside
inhibitor-binding pocket in the structure of the HIV-1 RT/α-APA
complex looking through a putative entrance to the pocket,
showing interactions between α-APA and nearby amino acid
residues. α-APA is shown in purple as a ball-and-stick model
with carbons purple, nitrogens cyan, oxygens red and bromines
magenta. The β7–β8 portion of p51 has a dashed outline. The
side chains are shown for the amino acid residues that make
close contacts with α-APA (in green), and for the three
essential aspartic acid residues D110, D185 and D186 (in red) at
the polymerase active site. Dashed lines indicate connections
between the side chains and the β-strands.
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