L coordination bond (black line), and two salt bridge (red-violet line
L coordination bond (black line), and two salt bridge (red-violet line) formation inside the catalytic pocket of mh-Tyr protein against co-crystallized reference ligand (Fig. S5). These outcomes support the considered docking grid and also other parameters as perfect for the evaluation of chosen flavonoids with mh-Tyr. Following, the XP docking of chosen flavonoids yields the highest binding affinities in between – 9.346 to – five.301 kcal/mol against the ARB inhibitor (- 5.795 kcal/mol) with mh-Tyr (Table S1, Fig. 2). Thus, the bestdocked poses of mh-Tyr with respective compounds at highest unfavorable docking scores had been selected for further intermolecular interaction evaluation. As depicted in Fig. two, all of the functional groups on A, B, and C-ring of 3 flavonoids, viz. C3G, EC, and CH, showed differential interactions together with the catalytic center of mh-Tyr containing binuclear copper ions (CuA400 and CuB401) by comparison towards the ARB inhibitor. Herein, mh-Tyr-C3G docked complicated was noted for the highest docking score of -9.346 kcal/mol and exhibited four hydrogens (H)-bonds at Gly281 (C=OH, OH of Glycosyl-ring in C3G: two.03 , Arg268 (N-HO, OH of Glycosyl-ring in C3G: 2.06 , and Glu322 (2; C=OH, OH of B-ring in C3G:1.97 and C=OH, OH of B-ring in C3G: 2.20 residues, and interactions with the binuclear copper ions (Cu400 and Cu401) by means of salt bridge formation at deprotonated hydroxyl group within the A-ring of C3G. Furthermore, hydrophobic (Val248, HSP Formulation Phe264, and Val283), polar (His61, His85, Hie244: histidine neutral -protonated, His259, Asn260, His263, and Ser282), optimistic (Arg268), unfavorable (Glu322), glycine (Gly281), and – (formation through A-ring in C3G with His85 and His263 residues) intermolecular contacts have been also noted within the mh-Tyr-C3G docked complicated (Fig. 2a,b). Likewise, molecular docking of EC with the mh-Tyr revealed -6.595 kcal/mol docking energy, contributed by metal coordination bond (Cu400) formation at deprotonated hydroxyl group in B-ring of EC as well as other intermolecular interactions, which includes hydrophobic (Phe90, Cys83, Val248, Phe264, Met280, Val283, Ala286, and Phe292), polar (His61, His85, His244, His259, Asn260, His263, and Ser282), glycine (Gly281), and – bond formation by means of B-ring in EC (His85, His259, and His263) interactions (Fig. 2c,d). Similarly, the mh-Tyr-CH docked complex was marked for – five.301 kcal/mol and formed two hydrogen bonds with Asn260 (C=OH, OH of C-ring in CH: two.02 and Gly281 (C=OH, OH of A-ring in CH: two.02 residues. Furthermore, salt bridge (Cu400 and Cu401), metal coordination bond (Cu400 and Cu401), hydrophobic (Phe90, Val248, Phe264, Pro277, Met280, Val283, Ala286, and Phe292), polar (His61, His85, His94, His244, His259, Asn260, His263, Ser282, and His296), optimistic (Arg268), adverse (Glu256), and Glycine (Gly281), bond formation via B-ring (His259 and His263) and A-ring (Phe264), and -cation bond formation by means of A-ring (Arg268) contacts had been also recorded within the mh-Tyr-CH docked complex (Fig. 2e,f). Nonetheless, molecular docking of ARB inhibitor within the active pocket from the mh-Tyr showed a relatively less adverse docking score (- 5.795 kcal/mol) and contributed by single H-bond at Asn260 (C=OH, OH of Glycosyl-ring in ARB: 1.73 , hydrophobic (Phe90, Val248, Monocarboxylate Transporter web Met257, Phe264, Met280, Val283, Ala286, and Phe292), polar (His61, His85, Hie244: histidine neutral -protonated, His259, Asn260, His263, and Ser282), negative (Glu256), glycine (Gly281), and – bond at phenol-ring of ARB (Phe264) interactions (Fig. 2g,h). Of note, all.