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. 2017 Mar 9;40(3):325–342. doi: 10.1007/s10545-017-0029-3

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© The Author(s) 2017

Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Fig. 2 — Crystallographic structure of human GALT. Cartoon representation of uridylylated human GALT crystallographic structure obtained in complex with galactose-1-phosphate (PDB code 5IN3). Each monomer is colored either in cyan or light orange. Active site residues H184-P185-H186 in red sticks; covalently linked UMP in blue sticks; galactose 1-phosphate in yellow sticks; residue Q188, responsible for UMP stabilization and site of the most common mutation (Q188R) in classic galactosemia in green sticks; zinc (purple sphere) binding ligands in gray sticks