|
Figure 3.
Fig. 3. Interaction of Met90'and Asp25' in PR[L90M]. (A)
The 2Fo–Fc electron density map showing Met90', Asp25' and
Thr26'in the PR[L90M] structure. The side chain of Met90' has
two conformations, and one conformation has a short separation
from the carbonyl oxygen of the catalytic Asp25'. (B) Comparison
of Met90' in PR[L90M] and Leu90' in the wild-type HIV-1 protease
(PR) relative to Asp25'. The PR residues are in black and the
PR[L90M] residues are in gray. Hydrogen bonds are indicated by
dashed lines, with the distances shown in Å.
|
