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Structural characterization of enzyme-inhibitor complexes revealed the original binding mode of these novel NAD mimics.
Molecular docking provided insight into the binding mode of these inhibitors and rationalized their different potencies.
This indicated differences in the binding mode of these compounds with APN and APA.
In addition, molecular modeling studies unravelled the binding mode of these inhibitors.
The anticipated binding mode of these analogs was confirmed by performing the in silico docking experiments.
Structure-activity relationships and docking studies confirmed the binding mode of these inhibitors within the ATP binding pocket of TgCDPK1.
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Molecular docking studies have provided possible binding modes of these inhibitors.
Molecular docking study was also carried out to understand the binding modes of these compounds.
Molecular docking studies revealed the binding modes of these compounds for Topo I and Topo II.
Docking studies showed that the binding modes of these compounds were consistent with the crystal structures of known inhibitors.
Our results revealed significantly different binding modes of these two inhibitors although both established extensive interaction networks with CCR5.
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