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Crystallization (Commentary)
Reference
1.14.14.17
analysis of the terbinafine-squalene epoxidase mode of interaction by docking studies followed by molecular dynamics simulations and quantum interaction energy calculations. In the energetically most likely orientation of terbinafine its interaction energy with the protein is ca. 120 kJ/mol. In the favorable position the terbinafine lipophilic moiety is located vertically inside the squalene epoxidase binding pocket with the tert-butyl group oriented toward its center, resulting in squalene epoxidase conformational changes and preventing the natural substrate from being able to bind to the enzyme's active site. Strongest interaction between terbinafine and squalene poxide stems from hydrogen bonding between hydrogen-bond donors, hydroxyl group of Tyr90 and amine nitrogen atom of terbinafine
715725
1.14.14.17
homology model of enzyme based on p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens
671379
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