Journal of Computer-Aided Molecular Design

, Volume 10, Issue 4, pp 293–304

Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4

Authors

  • Garrett M. Morris
    • Department of Molecular Biology, MB-5The Scripps Research Institute
  • David S. Goodsell
    • Department of Molecular Biology, MB-5The Scripps Research Institute
  • Ruth Huey
    • Department of Molecular Biology, MB-5The Scripps Research Institute
  • Arthur J. Olson
    • Department of Molecular Biology, MB-5The Scripps Research Institute
Research Papers

DOI: 10.1007/BF00124499

Cite this article as:
Morris, G.M., Goodsell, D.S., Huey, R. et al. J Computer-Aided Mol Des (1996) 10: 293. doi:10.1007/BF00124499

Summary

AutoDock 2.4 predicts the bound conformations of a small, flexible ligand to a nonflexible macromolecular target of known structure. The technique combines simulated annealing for conformation searching with a rapid grid-based method of energy evaluation based on the AMBER force field. AutoDock has been optimized in performance without sacrificing accuracy; it incorporates many enhancements and additions, including an intuitive interface. We have developed a set of tools for launching and analyzing many independent docking jobs in parallel on a heterogeneous network of UNIX-based workstations. This paper describes the current release, and the results of a suite of diverse test systems. We also present the results of a systematic investigation into the effects of varying simulated-annealing parameters on molecular docking. We show that even for ligands with a large number of degrees of freedom, root-mean-square deviations of less than 1 Å from the crystallographic conformation are obtained for the lowest-energy dockings, although fewer dockings find the crystallographic conformation when there are more degrees of freedom.

Keywords

InhibitorReceptorSimulated annealingDrug design

Copyright information

© ESCOM Science Publishers B.V 1996