S to residue Y355 (341), 4 compounds to residue R120 (106) and three compounds to residue Y385 (371). For the structures of those seven compounds, three of them contained extended carbon chain structures (DA108, DA114 and DA164) and 3 of them contained aromatic rings (DA175, DB019 and ZF04). Three compounds formed H-bonds among their ester groups and residues (DA164, DA175 and DB019), two compounds formed H-bonds with surroundings via their aldehyde groups (DA114 and DA175), two compounds by means of hydroxyl groups (DB019 and F04), one particular compound via carboxyl group (DA108) and 1 compound through its amidogen group (ZF04). Lastly, 14 compounds formed H-bonds with only one of the essential active site residues. Seven of them contained aromatic rings (DA012, DA053, DA134, DA216, DB004, DB005 and DA024) as well as the other people contained extended carbon chain structures (DA145, DA153, DA165, DA172, DA173, DA196 and ZF02). Additionally, 13 compounds had been Imidazoline Receptor list located to form H-bonding to residue Y385 (371), 1 compound to residue R120 (106) and none to residue Y355 (341). In seven compounds, including DA053, DA134, DA165, DA172, DA173, DA196 and DA216, H-bonds were identified involving aldehyde groups plus the surrounding residues. 5 compounds, like DA012, DA153, DB004, DB005 and DB024, formed H-bonds with surrounding residues by way of their ester groups. Furthermore, H-bonds had been identified in between hydroxyl groups in DA145 and R120 (106) and among carboxyl groups in ZF02 and Y385 (371). Comparing the above structures using the identified inhibitor of PTGS2, salicylate (aspirin), which has an aromatic ring using a carboxyl and an ester group, some similarities may very well be identified (Fig. 4c)42. The structures of ten compounds had aromatic rings, including DA012, DA053, DA134, DA175, DA216, DB004, DB005, DB019, DB024 and ZF04. A total of eight compounds had ester groups (DA012, DA153, DA164, DA175, DB004, DB005, DB019 and DB024) and three compounds involved carboxyl (DA108, DC012 and ZF02). However, the top 5 binding affinity compounds of PTGS2 have been KA090, ZC12, KB031, KA113 and KA091, whereas in the active binding web-sites, the top rated five binding affinity compounds have been KA120, DA064,Scientific Reports | Vol:.(1234567890)(2021) 11:6656 |https://doi.org/10.1038/s41598-021-86141-www.nature.com/scientificreports/Figure four. Ligand arget interactions for compounds forming hydrogen bonds with catalytic triad residues of prostaglandin-endoperoxide synthase two. (a) Compounds forming hydrogen bonds with three catalytic triad residues. (b) Compounds forming hydrogen bonds with two catalytic triad residues. (c) Structure of inhibitor of prostaglandin-endoperoxide synthase 2, salicylate (aspirin). DA108 tetradecanoic acid, DA114 10-undecenal, DA164 trans,trans-2,4-hexadienyl acetate, DA175 5-acetoxymethylfurfural, DB019 senkyunolide F, DC012 azelaic acid, ZF04 tyrosine. ZC07, DA084 and DA012. These compounds come from all 3 herbs of the formula, indicating that the effects from the compounds in the herbal formula might be superior to these from the compounds from any single herb. Even so, binding affinity values alone may not be totally precise as an indicator of prospective biological activity, since they could have errors of up to two kcal/mol43. Therefore, an inspection from the number of powerful non-covalent interactions amongst ligands and binding web pages should also be used to predict possible bio-activities of herbal compounds, a basic strategy previously employed in analyses of α9β1 Storage & Stability molecular docking.