Ontology highlight
ABSTRACT:
SUBMITTER: Rueda M
PROVIDER: S-EPMC2811216 | biostudies-literature | 2010 Jan
REPOSITORIES: biostudies-literature
Rueda Manuel M Bottegoni Giovanni G Abagyan Ruben R
Journal of chemical information and modeling 20100101 1
The use of multiple X-ray protein structures has been reported to be an efficient alternative for the representation of the binding pocket flexibility needed for accurate small molecules docking. However, the docking performance of the individual single conformations varies widely, and adding certain conformations to an ensemble is even counterproductive. Here we used a very large and diverse benchmark of 1068 X-ray protein conformations of 99 therapeutically relevant proteins, first, to compare ...[more]