title: Binding dynamics of two water molecules constrained within the scytalone dehydratase binding pocket.
abstract: Two water molecules reside between inhibitors and active site residues of scytalone dehydratase. A molecular dynamics study is consistent with one water molecule binding less tightly than the other. Inhibitor binding studies with site-directed mutants indicate that the hydrogen bonding network around the less mobile water molecule contributes much greater binding energy than that around the more mobile one.
authors.affiliation: E. I. DuPont de Nemours Agricultural Products, Stine-Haskell Research Center, Newark, DE 19714, USA.
authors.forename: D B
authors.initials: DB
authors.lastname: Jordan
authors.forename: G S
authors.initials: GS
authors.lastname: Basarab
mesh_terms: D001665:Binding Sites; D003198:Computer Simulation; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000378:metabolism; D006836:Hydro-Lyases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008956:Models, Chemical; D016297:Mutagenesis, Site-Directed; D012457:Salicylamides / Q000378:metabolism; D013816:Thermodynamics; D014867:Water / Q000737:chemistry / Q000378:metabolism*
chemical_list: D004791:Enzyme Inhibitors; D012457:Salicylamides; D014867:Water; D006836:Hydro-Lyases; C082741:scytalone dehydratase; C031060:salicylamide