Validation of ligands in macromolecular structures determined by X-ray crystallography.

ABSTRACT: Crystallographic studies of ligands bound to biological macromolecules (proteins and nucleic acids) play a crucial role in structure-guided drug discovery and design, and also provide atomic level insights into the physical chemistry of complex formation between macromolecules and ligands. The quality with which small-molecule ligands have been modelled in Protein Data Bank (PDB) entries has been, and continues to be, a matter of concern for many investigators. Correctly interpreting whether electron density found in a binding site is compatible with the soaked or co-crystallized ligand or represents water or buffer molecules is often far from trivial. The Worldwide PDB validation report (VR) provides a mechanism to highlight any major issues concerning the quality of the data and the mode

SUBMITTER: Smart OS 

PROVIDER: S-EPMC5947763 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature