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. Author manuscript; available in PMC: 2017 Mar 31.
Published in final edited form as: Catalysts. 2016 May 27;6(6):81. doi: 10.3390/catal6060081

Figure 3.

Figure 3

Location of drug resistance and conformational mutations in HIV-1 PR. Structural mapping of various mutations on the crystal structure of apo HIV-1 PR (1HHR). The catalytic Asp25 residue is depicted as cyan sticks on each enzyme protomer. All spheres represent a residue documented to undergo mutation in HIV-1 PR [97]. (a) Location of drug resistance-inducing mutations. Magenta spheres represent mutations that impair inhibitor binding through direct active-site contacts (primary mutations) and gray spheres represent distal indirect mutations (secondary mutations); (b) Location of mutations documented to affect the conformational sampling of HIV-1 PR, depicted as orange spheres. Gray spheres are other drug resistance-inducing mutations. All mutations were compiled from references listed in the text.