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EC Number
Metals/Ions
Commentary
Reference
Ca2+
not required for activity, one calcium ion is located at the N-terminal region of helix alphaA-1, and is coordinated by the backbone carbonyl of Lys22 and the Glu26 carboxylate, Asp25 carboxylate contributes to the calcium binding via one of the coordinating water molecules. Another calcium ion is bound in a crystal packing interface between chain A and chain C' of a crystallographic symmetry-related hexamer and is coordinated by the carboxylates of GluA45 and AspA58 from one chain and the carboxylate from Glu C'45 (bidentate coordination) of the symmetry-related chain with three water molecules completing a capped-octahedral coordination sphere
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no significant stimulation or reduction of enzyme activity in the presence of divalent metal ions or EDTA. In the paraoxon-bound structure, the diethylphosphate moiety is stabilized by hydrogen-bonding interactions with the oxyanion hole. One of the two ethyl arms of bound paraoxon points toward the larger pocket in the protein, while the other follows the groove of the small pocket. The two ethyl arms are stabilized by packing against Tyr92, Trp124, Pro228, Ile276, and His303
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