Figure 4.
Structural mapping and interaction network of the gilteritinib-resistant mutations in FLT3. The residues for which mutations have been identified from the in vitro saturation mutagenesis screen are represented as spheres. Gilteritinib is shown as a ball-and-stick model. All of atoms are colored by the type of element (white: hydrogen; cyan, gray, and orange: carbon; blue: nitrogen; red: oxygen, yellow: sulfur). For clarity, the hydrogen atoms are omitted. Molecular interactions are shown as dotted lines and colored by the type of interaction (cyan: hydrogen bond; yellow: via van der Waals interaction; light green: CH−π interaction). (A) Gilteritinib bound to FLT3. The residues in front of the gatekeeper residue F691 is hidden. (B) Another view of gilteritinib bound to FLT3. The hydrogen atoms of G697 are shown.

Structural mapping and interaction network of the gilteritinib-resistant mutations in FLT3. The residues for which mutations have been identified from the in vitro saturation mutagenesis screen are represented as spheres. Gilteritinib is shown as a ball-and-stick model. All of atoms are colored by the type of element (white: hydrogen; cyan, gray, and orange: carbon; blue: nitrogen; red: oxygen, yellow: sulfur). For clarity, the hydrogen atoms are omitted. Molecular interactions are shown as dotted lines and colored by the type of interaction (cyan: hydrogen bond; yellow: via van der Waals interaction; light green: CH−π interaction). (A) Gilteritinib bound to FLT3. The residues in front of the gatekeeper residue F691 is hidden. (B) Another view of gilteritinib bound to FLT3. The hydrogen atoms of G697 are shown.

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