A theoretical study on the characteristics of the intermolecular interactions in the active site of human androsterone sulphotransferase: DFT calculations of NQR and NMR parameters and QTAIM analysis
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- 作者：Elahe K. Astania ; Emran Heshmatib ; Chun-Jung Chenc ; Nasser L. Hadipoura ; hadipour@modares.ac.ir" class="auth_mail" title="E-mail the corresponding author
- 关键词：Active site ; SULT2A1/ADT ; ADT ; DFT ; Noncovalent intermolecular interactions ; EFG and CS tensors ; QCC and CS parameters ; NBO and QTAIM analyses
- 刊名：Journal of Molecular Graphics and Modelling
- 出版年：2016
- 出版时间：July 2016
- 年：2016
- 卷：68
- 期：Complete
- 页码：14-22
- 全文大小：1400 K
文摘
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A theoretical study at the level of the density functional theory (DFT) was performed to characterize noncovalent intermolecular interactions, especially hydrogen bond interactions, in the active site of enzyme human androsterone sulphotransferase (SULT2A1/ADT).
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Results revealed that androsterone (ADT) is able to form hydrogen bonds with residues Ser80, Ile82, and His99 of the active site.
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Also, ADT involves in electrostatic and Van der Waals interactions with residues Phe18, Pro43, Lys44, Trp72, Phe133, and Trp134 of this active site.