GRaSP: a graph-based residue neighborhood strategy to predict binding sites

Abstract

Abstract Motivation The discovery of protein–ligand-binding sites is a major step for elucidating protein function and for investigating new functional roles. Detecting protein–ligand-binding sites experimentally is time-consuming and expensive. Thus, a variety of in silico methods to detect and predict binding sites was proposed as they can be scalable, fast and present low cost. Results We proposed Graph-based Residue neighborhood Strategy to Predict binding sites (GRaSP), a novel residue centric and scalable method to predict ligand-binding site residues. It is based on a supervised learning strategy that models the residue environment as a graph at the atomic level. Results show that GRaSP made compatible or superior predictions when compared with methods described in the literature. GRaSP outperformed six other residue-centric methods, including the one considered as state-of-the-art. Also, our method achieved better results than the method from CAMEO independent assessment. GRaSP ranked second when compared with five state-of-the-art pocket-centric methods, which we consider a significant result, as it was not devised to predict pockets. Finally, our method proved scalable as it took 10–20 s on average to predict the binding site for a protein complex whereas the state-of-the-art residue-centric method takes 2–5 h on average. Availability and implementation The source code and datasets are available at https://github.com/charles-abreu/GRaSP. Supplementary information Supplementary data are available at Bioinformatics online.