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. 2009 Dec 10;38(5):1738–1748. doi: 10.1093/nar/gkp1093

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© The Author(s) 2009. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — The active site of HlAIPT. (A) Molecular surface of HlAIPT. The enzyme forms a central reaction channel. The cross-sectional surface, which is cut at the dashed line in (B), is colored light blue. The ball-stick model shows the side chains of Met64, Ser129 and Ser131. The ATP molecule and phosphate ion are shown as rods. (B) A cluster of positively charged residues surround the open end of the ATP-binding channel. (C) Stereoscopic view of ATP binding to the HlAIPT. Hydrogen bonds and charge–charge interactions are shown as dashed lines.