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Solvent Accessible Surface Area (SASA) was determined with the GetArea server [ 17 ]

Reference Protein and Structure Sequence P00390 (1.8.1.7) (Sequence Homologues) (PDB Homologues) Biological species Homo sapiens (Human) PDB 2gh5 - Crystal Structure of human Glutathione Reductase complexed with a Fluoro-Analogue of the Menadione Derivative M5 (1.7 ) Catalytic CATH Domains 3.30.390.30 3.50.50.60 (see all for 2gh5) Cofactors Fadh2(2-) (1), Glutathione (1) Enzyme Reaction (EC:1.8.1.7) Alternative enzyme names: GSH reductase, GSSG reductase, NADPH-GSSG reductase, NADPH-glutathione reductase, NADPH:oxidized-glutathione oxidoreductase, Glutathione S-reductase, Glutathione reductase, Glutathione reductase (NADPH), Enzyme Mechanism Introduction Initially, the enzyme is in the oxidised state, with its redox active cysteines 58 and 63 forming a disulphide bond to each other

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Tepel M, van der Giet M, Schwarzfeld C, Laufer U, Liermann D, Zidek W

Along with genetic improvement, several gene therapies for the treatment of hemoglobinopathies are currently in clinical trials or under development, including therapies utilizing gene replacement therapy using lentiviruses and the latest gene editing techniques [86,87,88]