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Moreover, structural superposition between GSH-bound OsDHAR and glutathione disulphide (GSSG)-bound hGSTO1-1 showed dramatic helix (α5, α6 and α9) movement in the C-terminal domain region of OsDHAR, which likely allows bound GSH molecules in the G- and H-sites to be sufficient close for GSSG formation (Supplemental Fig

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