Binding mode study of cellopentaose in β-glucosidase B via docking simulation

Paenibacillus polymxca β-glucosidase b (bglb),belong to a gh family 1,is a monomeric enzyme that acts as an exo-β-glucosidase hydrolyzing cellobiose and cellooligosachharidess of higher degree of polymerization by cleaving β-1,4 glycosidic linkage exist between glucosyl residue. this study reports on binding modes between bglb with cellopentaose which consist of five glucosyl residue. several visual inspection and protein –ligand interaction analysis was focused on finding amino acid residue involve in each glucosyl residue.computational docking calculation was performed using program gold generating ten solution bglb-cellopentaose complexes. from visual inspection,subsite -1 record the most interacting residue namelygln22,asn166,glu167,asn296,glu356,trp402,glu409 and trp410. the reducing glycosyl at subsite +1 are making interacting with residue namely trp328,asn223 and his181. meanwhile,the residues arg243,leu174,gln316 and tyr169 making contact with reducing glycosyl at the subsite +2 and subsite +3. lastly,only two residues,his318 and glu180 reported to make interaction within reducing glycosyl at subsite +4 as it is already over exposed towards outside of binding cleft. from overall,a total of 11 hydrogen bonds were observed in bglb-cellopentaose complex © school of engineering,taylor’s university.