A STRUCTURAL SURVEY OF CATALYTIC RESIDUES AND RING CONFORMATIONS IN GLYCOSIDE HYDROLASES FROM THE CAZY DATABASE
Keywords:
Carbohydrate-Ligand Interactions, 3D Structure Analysis, Glycoside Hydrolase Families, Sugar Conformational AnalysisAbstract
In this study, we performed a comprehensive statistical analysis and a detailed survey of carbohydrate ligands bound within the active sites of carbohydrate-active enzymes (CAZymes) from the CAZy database (www.cazy.org). Specifically, we analyzed 3D structures of CAZyme-carbohydrate ligand complexes across 184 glycoside hydrolase families. By utilizing only coordinate files, we were able to retrieve, analyze, and interpret key structural and functional features. These include previously underexplored aspects, such as Cremer-Pople and Altona-Sundaralingam analyses of sugar ring conformations at the subsite -1 sugar ring, identification of catalytic residues (acid/base and nucleophile), and population trends. This study provides structural insights into catalytic residue patterns and ring conformational preferences in CAZymes, thereby supporting future efforts in functional analysis, mechanistic interpretation, and elucidation of catalytic itineraries.
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