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. 2019 Oct 24;6(Pt 6):1120–1133. doi: 10.1107/S2052252519012399

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© Ieva Drulyte et al. 2019

This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.

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Comparison of IdmH (blue) with its sequence and structural homologue SnoaL (pink). (a) IdmH chain A was aligned with SnoaL (PDB entry 1sjw) chain A using PyMOL. (b) Active-site residues in SnoaL (pink) compared with their counterparts in IdmH (blue). While some residues appear to be conserved between the two proteins (His129/His119, Trp63/Trp54 and Phe19/Phe19), the charged essential catalytic residues His107 and Asp121 are unique to SnoaL. Another difference between the two active sites arises from different choices and positioning of aromatic residues (Trp59/Tyr31 and Trp63/Trp54), while Tyr16 appears to be completely unique to IdmH. Asterisks denote SnoaL catalytic residues (Sultana et al., 2004 ▸).