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Altered Residues Affecting Cofactor Binding in hGALE Structures

This figure shows altered residues (N34S, G90E, K161N) affecting cofactor binding in UDP-Glc and UDP-GlcNAc bound hGALE structures. Original residues are deep teal, altered residues are pink. Oxygen, nitrogen, and phosphate atoms are colored red, blue, and orange. Created using PyMol with energy minimized structures of 1EK5 and 1HZJ.

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Altered Residues Affecting Cofactor Binding in hGALE Structures

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  1. Figure S3 – page 1 50%>X>20% X<20% X>50% Activity (UDP-Gal) A B C Figure S3Aligned structures of altered residues predicted to directly affect cofactor binding for both UDP-Glc and UDP-GlcNAc boundhGALE. (A) p.N34S. (B) p.G90E. (C) p.K161N. Original residues are coloured deep teal while altered residues are coloured pink. Highlighted residues, cofactors and substrates are depicted as stick figures. WT and mutant structures are depicted as cartoon figures and are coloured wheat and light blue respectively. Oxygen, nitrogen and phosphate atoms are coloured red, blue and orange respectively. Figures were created using PyMol (www.pymol.com) and the appropriate energy minimised structures of 1EK5 and 1HZJ.

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