1ocn | pdb_00001ocn

Mutant D416A of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS in complex with a cellobio-derived isofagomine at 1.3 angstrom resolution

spinqualitylabelsall models 1ocn, resolution 1.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ocn is a 1 chain structure with sequence from Humicola insolens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.31Å Ligands: BGC, CA, IFM, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GUX6_HUMIN Plays a central role in the recycling of plant biomass. The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed A cellobio-derived isofagomine glycosidase inhibitor (Ki approximately 400 nM) displays an unusual distorted 2,5B (boat) conformation upon binding to cellobiohydrolase Cel6A from Humicola insolens, highlighting the different conformational itineraries used by various glycosidases, with consequences for the design of therapeutic agents. Distortion of a cellobio-derived isofagomine highlights the potential conformational itinerary of inverting beta-glucosidases.,Varrot A, Macdonald J, Stick RV, Pell G, Gilbert HJ, Davies GJ Chem Commun (Camb). 2003 Apr 21;(8):946-7. PMID:12744312 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cellobiohydrolase 3D structures

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