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![[Figure 2]](ji5027fig2mag.jpg)
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Figure 2
Interactions of galactinol at the active site of the D383A mutant compared with galactose binding to Asp383 in the wild type. The structure of D383A in complex with galactinol is shown. (a) The galactosyl moiety of galactinol (yellow sticks) is bound at the −1 subsite. OD2 of Asp447 makes a direct interaction with O2 of the galactosyl moiety at a distance of 3.36 Å. Lys75, Trp78, Asp346, Asp446 and Tyr449 (green sticks) are involved in stabilization of the myo-inositol moiety by hydrogen-bonding interactions at the +1 subsite. Water molecules are shown as cyan spheres. (b) The carbon ring of the galactosyl moiety (yellow) of galactinol is distorted from that of galactose (green) bound to Asp383; the O3 and O4 groups hence interact with a different residue, Lys381, at the catalytic site as shown in (a). |
![[Figure 2]](ji5027fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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