How Diverse Are the Protein-Bound Conformations of Small-Molecule Drugs and Cofactors?

ABSTRACT: Knowledge of the bioactive conformations of small molecules or the ability to predict them with theoretical methods is of key importance to the design of bioactive compounds such as drugs, agrochemicals, and cosmetics. Using an elaborate cheminformatics pipeline, which also evaluates the support of individual atom coordinates by the measured electron density, we compiled a complete set ("Sperrylite Dataset") of high-quality structures of protein-bound ligand conformations from the PDB. The Sperrylite Dataset consists of a total of 10,936 high-quality structures of 4,548 unique ligands. Based on this dataset, we assessed the variability of the bioactive conformations of 91 small molecules-each represented by a minimum of ten structures-and found it to be largely independent of the number of

SUBMITTER: Friedrich NO 

PROVIDER: S-EPMC5880911 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature