Distortion of a cellobio-derived isofagomine highlights the potential conformational itinerary of inverting β-glucosidasesElectronic supplementary information (ESI) available: details of data and structure quality for complex of cel6A with 1. See http://www.rsc.org/suppdata/cc/b3/b301592k/

Abstract
A cellobio-derived isofagomine glycosidase inhibitor (Ki ∼ 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.

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