Phytoene desaturase(PDS) is the target of the bleaching herbicide,norflurazon.The the 2D and 3D structures of wild PDS and two mutations were achived by online prediction,docking of PDS and norflurazon was carried out by DOCK6.5.Binding stablity was analysed by molecular dynamics simulation via the software Gromacs.The energy changes and distribution were revealed by mm_pbsa.pl tools in Amber9.At last,important amino acids were confirmed by the analysis of hydrogen bond with LIGPLOT+. The results suggested that different mutations didn’t change the 2D and 3D structures of PDS,but mutated PDS showed higher RMSD,which indicated lower binding stablity,and higher bingding energy,which indicated the difficulity to bind to noflurazon .Our research might explain the mechanisms of the resistance to norflurazon.
