6JXG

Crystasl Structure of Beta-glucosidase D2-BGL from Chaetomella Raphigera

Summary for 6JXG

Entry DOI	10.2210/pdb6jxg/pdb
Descriptor	Beta-glucosidase, 2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose, ... (4 entities in total)
Functional Keywords	glucosidase, glycoside hydrolase, hydrolase
Biological source	Chaetomella raphigera
Total number of polymer chains	1
Total formula weight	76621.23
Authors	Wang, A.H.-J.,Lee, C.C.,Kao, M.R.,Ho, T.H.D. (deposition date: 2019-04-23, release date: 2019-11-20, Last modification date: 2023-11-22)
Primary citation	Kao, M.R.,Kuo, H.W.,Lee, C.C.,Huang, K.Y.,Huang, T.Y.,Li, C.W.,Chen, C.W.,Wang, A.H.J.,Yu, S.M.,Ho, T.H.D. Chaetomella raphigerabeta-glucosidase D2-BGL has intriguing structural features and a high substrate affinity that renders it an efficient cellulase supplement for lignocellulosic biomass hydrolysis. Biotechnol Biofuels, 12:258-258, 2019 Cited by PubMed Abstract: To produce second-generation biofuels, enzymatic catalysis is required to convert cellulose from lignocellulosic biomass into fermentable sugars. β-Glucosidases finalize the process by hydrolyzing cellobiose into glucose, so the efficiency of cellulose hydrolysis largely depends on the quantity and quality of these enzymes used during saccharification. Accordingly, to reduce biofuel production costs, new microbial strains are needed that can produce highly efficient enzymes on a large scale. PubMed: 31700541 DOI: 10.1186/s13068-019-1599-0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation