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The prediction of ion ligand–binding residues in protein sequences is a challenging work that contributes to understand the specific functions of proteins in life processes. In this article, we selected binding residues of 14 ion ligands as research objects, including four acid radical ion ligands and 10 metal ion ligands. Based on the amino acid sequence information, we selected the composition and position conservation information of amino acids, the predicted structural information, and physicochemical properties of amino acids as basic feature parameters. We then performed a statistical analysis and reclassification for dihedral angle and proposed new methods on the extraction of feature parameters. The methods mainly included applying information entropy on the extraction of polarization charge and hydrophilic–hydrophobic information of amino acids and using position weight matrices on the extraction of position conservation information. In the prediction model, we used the random forest algorithm and obtained better prediction results than previous works. With the independent test, the Matthew's correlation coefficient and accuracy of 10 metal ion ligand–binding residues were larger than 0.07 and 52%, respectively; the corresponding evaluation values of four acid radical ion ligand–binding residues were larger than 0.15 and 86%, respectively. Further, we classified and combined the phi and psi angles and optimized prediction model for each ion ligand–binding residue.

Recognizing Ion Ligand–Binding Residues by Random Forest Algorithm Based on Optimized Dihedral Angle