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![[Figure 3]](jc5013fig3mag.jpg)
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Figure 3
ManI and a Ca2+ ion bound in the catalytic active sites of BT3130 (a) and BT3965 (b). Ligands are shown together with the respective catalytic acid and base residues. The depicted electron-density maps are REFMAC maximum-likelihood/σA-weighted 2Fo − Fc syntheses contoured at 0.15 and 0.37 e Å−3 (1.0σ), respectively. (c) Extended overlay of the BT3130 (green) and BT3965 (orange) active-site pockets. Within the −1 subsite, all side chains, structural motifs and hydrogen-bonding interactions with ManI are fully conserved (rear centre of image, black labels). Structural elements that compose the reducing-end (positive) subsites show far greater variability (front left and upper right of image, grey labels). Enzyme–ligand/ion hydrogen bonds are shown as black dashed lines. |
![[Figure 3]](jc5013fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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