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. 2016 Jan 20;44(5):2417–2428. doi: 10.1093/nar/gkv1539

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© The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — RepDE and RepSTK1 share a common active site architecture. (A) The active site of RepDE. The structure reveals that the conserved residues of the Rep_trans family cluster around the catalytic tyrosine residue to form the active site. (B) The catalytic centre of RepSTK1 shows a remarkable conservation of structure between the two proteins with all of the side chains adopting identical conformations except R189 (R177 in RepSTK1). The electron density shown is anomalous difference density calculated from diffraction data collected at the Mn K-edge from a RepSTK1 crystal soaked in 10 mM MnCl₂, revealing the position of the metal ion in the active site. The structure shown was crystallized from a metal free solution where a water molecule (red sphere) occupies the metal binding site.