title: Docking and DFT studies on ligand binding to Quercetin 2,3-dioxygenase.
abstract: Simple molecular docking calculations on quercetin, kojic acid and diethylcarbamatodithoic acid using the software package MOE are shown to be close to the geometries reported in the X-ray crystal structures of the protein co-crystallized with the respective ligands. Furthermore, DFT optimization of the docked conformations is shown to reproduce the essential features of previous studies on quercetin, showing that docking can be used to provide good starting structures for mechanistic study. The flavone ligand, lacking the hydroxyl group of the quercetin is shown by docking to be unable to approach closely the copper atom, indicating the necessity of the presence of the hydroxyl group and providing a prediction of the likely binding environment of this ligand.
authors.affiliation: a Faculty of Science, Department of Chemistry , King Abdulaziz University , Jeddah 21589 , Saudi Arabia.
authors.forename: Aramice Y S
authors.initials: AY
authors.lastname: Malkhasian
authors.affiliation: b FEPS, Department of Chemistry , University of Surrey , Guildford , Surrey GU2 7XH , UK.
authors.forename: Brendan J
authors.initials: BJ
authors.lastname: Howlin
mesh_terms: D001665:Binding Sites; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D049308:Dioxygenases / Q000737:chemistry* / Q000378:metabolism; D047309:Flavones / Q000737:chemistry; D006860:Hydrogen Bonding; D008024:Ligands; D008968:Molecular Conformation; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D011794:Quercetin / Q000737:chemistry; D013329:Structure-Activity Relationship
chemical_list: D047309:Flavones; D008024:Ligands; D011794:Quercetin; D049308:Dioxygenases; C003281:quercetin 2,3-dioxygenase; C043562:flavone
keywords: DFT; docking; mechanism; quercetin