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Protein–Ligand Cocrystal Structures: We Can Do Better
Author(s) -
Charles H. Reynolds
Publication year - 2014
Publication title -
acs medicinal chemistry letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.065
H-Index - 66
ISSN - 1948-5875
DOI - 10.1021/ml500220a
Subject(s) - cocrystal , ligand (biochemistry) , crystallography , computer science , protein ligand , chemistry , hydrogen bond , molecule , biochemistry , receptor , organic chemistry
There is a large body of evidence that many protein-ligand cocrystal structures contain poorly refined ligand geometries. These errors result in bound structures that have nonideal bond lengths and angles, are strained, contain improbable conformations, and have bad protein-ligand contacts. Many of these problems can be greatly reduced with better refinement models.

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