Abstract
We report here the 2.5Å structure of HIV-1 protease tethered-dimer ritonavir complex. The inhibitor bound in the active site has different conformations in the two orientations. There is only one hydrogen bond between the inhibitor and the enzyme. The conserved flap-water is not found in the present complex.
Keywords: HIV-1 protease, tethered dimmer, inhibitor, X-ray crystallography