<p>Molecular docking predicted binding modes of (<b>A</b>) Ethyl 4-chloro acetoacetate, (<b>B</b>) Compound 278 (dark green sticks), Compound 73 (pale green sticks) and compound 23 (cyan sticks) with DHK protein. Active site, catalytic triad residues are highlighted with magenta and yellow colour sticks respectively. Substrate molecules in (<b>B</b>) panel were superimposed. NADPH molecule shown as cyan spheres. All the residues are labelled and hydrogen bonds specified as broken lines.</p
(A) Close-up stereo view of the substrate recognition site. Residues Q164, Q264, S370, and N393 form...
<p>Inhibitors are colored in cyan. The zinc ion is shown as a brown ball. Hydrogen bonds between HDA...
<p>(I) localization of potential kinase phosphorylation and PBD recognition motif; (a) Plk1-SMARCAD1...
<p>The binding modes (A) C15 (B) Hit 1 (C) Hit 2 and (D) Hit 3 at the active site of the enzyme. The...
<p>Stereoview of the docking of DDD32388 (cyan) into the active site of <i>Pa</i>FolD. Potentially i...
<p>Main receptor-interacting residues are labelled at their C-αatoms. Intermolecular hydrogen bonds ...
<p>View of the active site with NADH bound in the optimized position found by docking as described i...
<p>Ligands are shown as gray sticks; receptor residues are shown as green sticks. Bonds are shown wi...
<p>Experimental (A) and theoretical (B and C) binding mode of AdoHcy (A), <b>4</b> (B) and <b>14</b>...
The PK was shown in cartoon and colored gray. The ThDP, ligands, and 2 key residues R442 and K605 we...
<p>Active site residues are shown in stick form. PD00519 and compound 1 are color-coded: green – PD0...
<p><b>Panel A</b>: Docking pose of <b>1</b> in the OASS-A binding pocket. Red and green contours ide...
<p>Docking poses obtained for the two structurally-related compounds, (A) <b>RR4</b> (yellow) and (B...
<p>The 3D<b>-</b>EP24.15 structure focusing S-glutathiolated Cys residues is surface represented and...
<p>(A) The dThd binding site of <i>h</i>TK1 (lemon), <i>Lm</i>TK-dThd (light blue) and <i>Lm</i>TK-d...
(A) Close-up stereo view of the substrate recognition site. Residues Q164, Q264, S370, and N393 form...
<p>Inhibitors are colored in cyan. The zinc ion is shown as a brown ball. Hydrogen bonds between HDA...
<p>(I) localization of potential kinase phosphorylation and PBD recognition motif; (a) Plk1-SMARCAD1...
<p>The binding modes (A) C15 (B) Hit 1 (C) Hit 2 and (D) Hit 3 at the active site of the enzyme. The...
<p>Stereoview of the docking of DDD32388 (cyan) into the active site of <i>Pa</i>FolD. Potentially i...
<p>Main receptor-interacting residues are labelled at their C-αatoms. Intermolecular hydrogen bonds ...
<p>View of the active site with NADH bound in the optimized position found by docking as described i...
<p>Ligands are shown as gray sticks; receptor residues are shown as green sticks. Bonds are shown wi...
<p>Experimental (A) and theoretical (B and C) binding mode of AdoHcy (A), <b>4</b> (B) and <b>14</b>...
The PK was shown in cartoon and colored gray. The ThDP, ligands, and 2 key residues R442 and K605 we...
<p>Active site residues are shown in stick form. PD00519 and compound 1 are color-coded: green – PD0...
<p><b>Panel A</b>: Docking pose of <b>1</b> in the OASS-A binding pocket. Red and green contours ide...
<p>Docking poses obtained for the two structurally-related compounds, (A) <b>RR4</b> (yellow) and (B...
<p>The 3D<b>-</b>EP24.15 structure focusing S-glutathiolated Cys residues is surface represented and...
<p>(A) The dThd binding site of <i>h</i>TK1 (lemon), <i>Lm</i>TK-dThd (light blue) and <i>Lm</i>TK-d...
(A) Close-up stereo view of the substrate recognition site. Residues Q164, Q264, S370, and N393 form...
<p>Inhibitors are colored in cyan. The zinc ion is shown as a brown ball. Hydrogen bonds between HDA...
<p>(I) localization of potential kinase phosphorylation and PBD recognition motif; (a) Plk1-SMARCAD1...