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Figure 2
Alternative conformations of Asn44, Ser45 and the catalytic Asp104 upon mannose binding in the −1 subsite. Superposition of the apo structure of Uhgb_MP (PDB entry 4udi ) and Uhgb_MP complexed with mannose (PDB entry 4udj ), illustrating the movement of the catalytic residues when mannose is bound at the −1 subsite. The backbone of the apo form is shown in grey (A conformation), while the backbone of the complexed, catalytically active form (B conformation) is in green. Water, phosphate and glycerol molecules in the apo form are shown. 2FoFc electron-density maps are shown (contoured at 1.0σ) for the catalytic residues in the apo and mannose-bound forms. Interatomic distances are labelled in Å.

Journal logoBIOLOGICAL
ISSN: 1399-0047
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