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![[Figure 7]](gx5066fig7mag.jpg)
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Figure 7
Stereoview of the superposition of PfPNP–ino (light green), PfPNP–SO4 (only the sulfate is shown, in blue) and PfPNP–immucillin (yellow). The loop above the binding pocket of the immucillin-H complex structure is complete and shows a water-mediated bond between residues Asp218 and Asp206, whereas in the other two structures the loop is disordered or flexible and the model cannot be built. The PfPNP–immucillin structure shows a water-mediated interaction of Asp206 and Trp212 with the inhibitor. In PfPNP–ino, the substrate does not form these bonds and is shifted relative to immucillin-H, together with the aromatic residues Trp212 and Tyr160. |
![[Figure 7]](gx5066fig7.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
