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. 2020 Mar 12;25(6):1289. doi: 10.3390/molecules25061289

Table 1.

Computational predictions of interactions between ligands and MTase domain of human DNMT1 by molecular docking. Concordant amino acid residues involved in the predicted interactions are indicated in bold.

Ligand CID 2D
Molecular
Structures *		 Binding Energy
(Kcal/mol)		 Max RMSD ** Hydrophobic Contacts Hydrogen Bonds
S-adenosyl-homocysteine
(SAH)		 439155 graphic file with name molecules-25-01289-i001.jpg −8.3 4.547 Phe1145, Leu1151, Glu1168, Cys1191, Leu1247,
Ala1579, Val1580		 Met1169, Asp1190, Ans1578
caffeic acid 689043 graphic file with name molecules-25-01289-i002.jpg −6.7 6.809 Ser1146, Gly1147, Cys1148, Asn1578, Ala1579 Gly1149, Gly1150, Leu1151, Val1580
hydrocinnamic
acid		 107 graphic file with name molecules-25-01289-i003.jpg −5.2 7.170 Ser1146, Gly1147, Asn1578, Gly1223 Leu1151, Val1580
p-coumaric acid 637542 graphic file with name molecules-25-01289-i004.jpg −6.0 6.049 Gly1147, Asn1578, Ala1579 Gly1149, Gly1150, Leu1151, Val1580
(−)-epigallocatchin−3-gallate 65064 graphic file with name molecules-25-01289-i005.jpg −10.4 0.1564 Arg1312, Asn1578, Val1580, Gly1223,
Gly1147, Phe1145 		Glu1266, Arg1310

CID–PubChem Compound ID number; (*) Retrieved from ChemSpider (https://www.chemspider.com/Default.aspx); (**) RMSD-Root-Mean-Square Deviation.