Plumbagin (PL) binding to the cavity of Stat3.

<p>Panels A–C: show the (un)binding simulation phases of PL, 'A' is farthest from the binding site, 'B' is the closest to the binding site, and 'C' is the binding site phase. The hydrogen bonds are shown as green-dashed lines with indicated bond length and the residues involved in hydrophobic interactions are shown as red arcs. Those residues which are common to the last phase (C) are encircled. Panel D: Another representation for phase C. The whole protein is displayed in cartoon representation and PL in sticks colored as green. The interacting residues are labeled and shown as surface in different colors.</p

Plumbagin (PL) binding to the cavity of PI3Kγ.

<p>Panels A–F: show the (un)binding simulation phases of PL, 'A' is farthest from the binding site, 'E' is the closest to the binding site, and 'F' is the binding site phase. The hydrogen bonds are shown as green-dashed lines with indicated bond length and the residues involved in hydrophobic interactions are shown as red arcs. Those residues which are common to the last phase (F) are encircled. Panel G: Another representation for phase F. The whole protein is displayed in cartoon representation and the ligand molecules are in sticks; PL colored as green and the bound known inhibitor in blue. The interacting residues are labeled and shown as surface in different colors.</p

The binding strength of plumbagin (PL) with the five cancer signaling proteins is shown with number of molecular interactions and other scores.

<p>The number of residues involved in the hydrophobic interactions are provided in parentheses. The 'K_d' denotes the dissociation constant. The binding energy and −log(K_d) values are calculated using X-Score. The more negative is the Dock/Grid score, the better is the docking.</p

The computational tools which were used in this study are presented with their source and application.

<p>The computational tools which were used in this study are presented with their source and application.</p

Plumbagin (PL) binding to the cavity of NF-κB.

<p>Panels A-B: show the (un)binding simulation phases of PL, 'A' is farthest from the binding site and representing many stages always coming with 2 interacting residues and 'B' is the binding site phase. The hydrogen bonds are shown as green-dashed lines with indicated bond length and the residues involved in hydrophobic interactions are shown as red arcs. Those residues which are common to the last phase (B) are encircled. Panel C: Another representation for phase B. The whole protein is displayed in cartoon representation and PL in sticks colored as green. The interacting residues are labeled and shown as surface in different colors.</p