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. Author manuscript; available in PMC: 2022 Jan 1.
Published in final edited form as: Eur J Drug Metab Pharmacokinet. 2021 Jan;46(1):105–118. doi: 10.1007/s13318-020-00653-1

Fig. 9. Hydrophobic interaction and hydrogen bond analyses of the SULT1E1 allozymes.

Fig. 9.

Atoms interacted with Ala43 (A), Ala131 (B), Arg186 (C), Pro214 (D), and Asp220 (E) are colored by the blue-white-red gradient (left panels; WT). Estimated interaction formed with Asp43 in A43D (A), Pro131 in A131P (B), Leu186 in R186L (C), Thr214 in P214T (D), and Val220 in D220V (E) are colored by the blue-white-red gradient (right panels; substituted). Side-chain conformation of a substituted residue was simulated using the Dunbrack backbone-dependent rotamer library [36]. Hydrophobic and hydrogen bond interactions of the substituted residues were also simulated by Find Clashes/Contacts tool in USCF Chimera software [37]. Top five-ranked rotamers of each substituted residue are modeled using the Dunbrack backbone-dependent rotamer library [36] and interaction was analyzed by Find Clashes/Contacts tool in USCF Chimera software. Hydrogen bonds formed with Cys122 (C) and Arg200 (E) are shown by blue slid lines (left panels). 1Wild-type human SULT1E1; PAP, (3’-phosphoadenosine 5’-phosphate); E2, (17β-Estradiol).