EC Number   |
|---|
   3.2.1.207 | crystal structures of the catalytic alpha subunit complexed with two different glucosyl ligands containing the scissile bonds of first and second-step reactions. The nonreducing terminal disaccharide moieties of the two kinds of substrates can be accommodated in a gourd-shaped bilocular pocket |
| 3.2.1.207 | mannose 6-phosphate receptor homology domain of GII beta subunit bound to mannose, to 1.6 A resolution. No major difference in the overall fold of ligand-bound and unbound structures, but a repositioning of side chains throughout the binding pocket, including Y372 |
| 3.2.1.207 | 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 |
| 3.2.1.207 | structure of a complex formed between the alpha-subunit GIIa and the GIIa-binding domain of the beta-subunit GIIb. GIIa forms a heterodimeric structure through its distal C-terminal domain |
| 3.2.1.207 | structures of a trypsinolytic fragment, alone and in complex with catalytic cycle ligands, and four different broad-spectrum antiviral iminosugar inhibitors |
