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Figure 3
Structure of AoAA13-G2(α1,4). (a) The AoAA13-G2(α1,4) structure (green) interacting with maltose along with a symmetry-related molecule (white) involved in crystal contacts near the active site. (b) Disorder of the AoAA13-G2(α1,4) metal-binding site with the metal-binding residues in two conformations and the 2FoFc map in blue. (c) Electron density for the maltose ligand [2Fo − Fc map (blue) and FoFc map (green)] calculated prior to incorporation of the ligand. In both (b) and (c) the 2FoFc and FoFc maps are contoured at 1σ and 3σ, respectively. (d) Principal protein–ligand interactions in AoAA13-G2(α1,4) and the position of maltose relative to the His brace. Direct and water-mediated interactions (red spheres) with Arg53 and Ser188 (green sticks) are shown. A symmetry-related maltose molecule (white) interacting with the β5–β6 loop is also shown. Zn-AoAA13 is shown for comparison (grey).

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
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