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Figure 1
Overall structure of wild-type StoMGMT. The protein is shown as a ribbon diagram with the NTD (residues 1–55) colored cyan, the connecting loop colored purple and the CTD (residues 70–156) colored green. β indicates β-strand, while h and H indicate 310-helix and α-helix, respectively. The Cys29–Cys31 disulfide bond is found in two different conformations. The sulfate ions are shown using a ball-and-stick model. H9 is ordered in the structures of the C120S and Y91F mutants.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 77| Part 12| December 2021| Pages 444-451
https://doi.org/10.1107/S2053230X21011055
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