Crystal structure of human sex hormone-binding globulin (SHBG) in ribbon form representation co-complexed with dihydrotestosterone (DHT) (left panel) and two dimensional representation of DHT (right panel).

<p>Crystal structure of human sex hormone-binding globulin (SHBG) in ribbon form representation co-complexed with dihydrotestosterone (DHT) (left panel) and two dimensional representation of DHT (right panel).</p

Nomenclature, commonly used abbreviations, and PubChem IDs of the ligands for docking study with human sex hormone-binding globulin (SHBG).

<p>Nomenclature, commonly used abbreviations, and PubChem IDs of the ligands for docking study with human sex hormone-binding globulin (SHBG).</p

Amino-acid residues in the binding pocket of human sex hormone-binding globulin (SHBG) involved in interactions with di-iso-decyl phthalate (DIDP) and natural ligand, dihydrotestosterone (DHT).

<p>Amino-acid residues in the binding pocket of human sex hormone-binding globulin (SHBG) involved in interactions with di-iso-decyl phthalate (DIDP) and natural ligand, dihydrotestosterone (DHT).</p

Amino-acid residues in the binding pocket of human sex hormone-binding globulin (SHBG) involved in interactions with dimethyl phthalate (DMP), dibutyl phthalate (DBP), di-iso-butyl phthalate (DIBP), butylbenzyl phthalate (BBP).

<p>Amino-acid residues in the binding pocket of human sex hormone-binding globulin (SHBG) involved in interactions with dimethyl phthalate (DMP), dibutyl phthalate (DBP), di-iso-butyl phthalate (DIBP), butylbenzyl phthalate (BBP).</p

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

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

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

Comparative binding analysis of A: natural ligand testosterone (TST) with B: bisphenol A (BPA), C: methylbishydroxyphenylpentene (MBP), and D: 4-tert-octylphenol (OP) in the binding site of human androgen receptor (AR).

<p>The hydrogen bonds are shown as green-dashed lines with indicated bond lengths and the residues involved in hydrophobic interactions are shown as red arcs. The interacting residues which are common for all the ligands are encircled.</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