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Figure 2.
Fig. 2. Positioning of the inhibitor in the active site and
hydrogen-bond network. One of the inhibitor hydroxyls has
extensive contacts with the catalytic Asp25/Asp125. The
hydrogen-bond distances are short (2.7–2.8 Å). The
gauche hydroxy group is hydrogen-bonded to one of the catalytic
aspartate residues. Gly27/Gly127 contribute to the active-site
hydrogen-bond network by donation of hydrogens via the
main-chain amide groups. These two compounds 1 and 2 represent
the two groups of inhibitors in this study. Compound 1 (A) has
10 and compound 2 (B) has 8 hydrogen-bond donors/acceptors. In
the latter case, two water molecules remain co-ordinated to the
G48/G148 carbonyl groups after complex formation.
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