idelalisib (seeNote 3). To do this, open the original PI3Kδstruc-
ture in Chimera by going toFile!Fetch by IDand writing its PDB
code (4XE0) at the blank field. If all steps were performed correctly,
the top-scoring conformation should be very similar to the crystal-
lographic one (root mean square deviation, RMSD¼0.374 A ̊), as
shown in Fig.3b.Fig. 3(a) Analysis of the hydrogen bond interactions for a predicted PI3Kδ-idelalisib complex. (b) Comparison
of the best docking solution (lowest energy) with the crystallographic conformation of idelalisib. The RMSD
between the predicted and experimental models is 0.374 A ̊. The protein backbone is in cartoon representation.
The ligand, water and residues in the binding site are depicted as sticks
44 Ricardo N. dos Santos et al.