journal menu
![[Figure 3]](ud5027fig3_combined_mag.jpg)
|
|
Figure 3
Side-by-side view of experimental and predicted binding poses. Shown are the binding poses of the starting fragments (left column), the docked poses of the follow-up ligands (middle column) and the binding poses of the follow-up ligands superimposed on polder OMIT mFo − DFc electron-density maps (Liebschner et al., 2017  ) contoured at σ = 3.0 (right column) as observed in the crystal structures for all ten follow-up ligand structures. (a) Fragment F005 and follow-up ligands. (b) Fragment F058 and follow-up ligands. (c) Fragments F066 and F290 and the respective follow-up ligands. (a, b, c) For comparison of the docking poses to the original crystallographic fragment pose, all views are identical, except for FU58-2 and FU66-1. For the latter, the crystallographic binding poses are also shown (purple sticks) to allow a comparison of the deviating binding poses. For the docking poses, favorable and unfavorable contact distances (green and red lines) and per-atom contributions to the overall DrugScoreX score (green and red spheres, with a radius approximating the score contribution), as predicted by DSX (Neudert & Klebe, 2011a), are highlighted. For the crystal structures, polar interactions are shown as dashed lines. Ligands (yellow) and interacting residues (gray) are depicted as sticks with standard color-coding for heteroatoms and are labeled in single-letter code. Only primary binding poses near the catalytic dyad are depicted. |
![[Figure 3]](ud5027fig3_combined.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
