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. 2009 Sep 14;423(Pt 1):15–22. doi: 10.1042/BJ20090826

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© 2009 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (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.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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(A) Crystal structure of TSAR (tartronic semialdehyde reductase) and its substrate analogue tartaric acid (TA) (PDB entry: 1VPD). (B) Predicted structure of GLYR1 generated by the fold-recognition server PHYRE (http://www.sbg.bio.ic.ac.uk/phyre/) using TSAR as a template. (C and D) Overlapping positions and identities of the predicted active-site residues for TSAR and GLYR1 respectively. Red, blue and green indicate negative, positive and hydrophobic regions of the residues.