Mining anion-aromatic interactions in the Protein Data Bank.

ABSTRACT: Mutual positioning and non-covalent interactions in anion-aromatic motifs are crucial for functional performance of biological systems. In this context, regular, comprehensive Protein Data Bank (PDB) screening that involves various scientific points of view and individual critical analysis is of utmost importance. Analysis of anions in spheres with radii of 5 Å around all 5- and 6-membered aromatic rings allowed us to distinguish 555 259 unique anion-aromatic motifs, including 92 660 structures out of the 171 588 structural files in the PDB. The use of a scarcely exploited (x, h) coordinate system led to (i) identification of three separate areas of motif accumulation: A - over the ring, B - over the ring-substituent bonds, and C - roughly in the plane of the aromatic ring, a

SUBMITTER: Kuzniak-Glanowska E 

PROVIDER: S-EPMC8985504 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature