Literature summary for 3.2.1.207 extracted from

Caputo, A.; Alonzi, D.; Marti, L.; Reca, I.; Kiappes, J.; Struwe, W.; Cross, A.; Basu, S.; Lowe, E.; Darlot, B.; Santino, A.; Roversi, P.; Zitzmann, N.
Structures of mammalian ER α-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals (2016), Proc. Natl. Acad. Sci. USA, 113, E4630-E4638 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
small-angle X-ray scattering and crystal structures of enzyme alone and in complex with key ligands of its catalytic cycle and antiviral iminosugars. A conformational rearrangement is needed for the simultaneous binding of a monoglucosylated glycan to both subunits. An insertion between the +1 and +2 subsites contributes to the enzyme's activity and substrate specificity, and the presence of D-mannose at the +1 subsite renders the acid catalyst less efficient during the cleavage of the monoglucosylated substrate	Mus musculus

Crystallization (Comment)

Organism

small-angle X-ray scattering and crystal structures of enzyme alone and in complex with key ligands of its catalytic cycle and antiviral iminosugars. A conformational rearrangement is needed for the simultaneous binding of a monoglucosylated glycan to both subunits. An insertion between the +1 and +2 subsites contributes to the enzyme's activity and substrate specificity, and the presence of D-mannose at the +1 subsite renders the acid catalyst less efficient during the cleavage of the monoglucosylated substrate

Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q8BHN3	-	-

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Release 2023.1 (January 2023)