Thioredoxin Glutathione Reductase

spinqualitylabelsall models Thioredoxin glutathione reductase with cofactor FAD dimer complex with triethylene glycol 2x8c Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Thioredoxin Glutathione Reductase (TGR) is an enzyme which bridges two detoxification pathways. It is composed of a small glutaredoxin domain at the N-terminal and a large thioredoxin reductase one at the C-terminal. Relevance TGR is a therpeutic drug target against the parasitic disease schistosomiasis. Structural highlights The active site of TGR contains CXXXXC motif and FAD.

3D Structures of Thioredoxin Glutathione Reductase

Updated on 21-December-2023

2v6o, 2x8c, 2x8g, 2x8h, 2xbi, 2xbq, 6ftc – SmTGR + FAD – Schistosoma mansoni
2x99 - SmTGR + FAD + NADPH
3h4k - SmTGR + FAD + auranofin
6rtj, 6rtm, 6rto, 6zlb, 6zlp, 6zp3, 6zst, 7b02, 7npx - SmTGR+FAD + inhibitor
8a1r - SmTGR+FAD + inhibitor – Cryo EM
6fmu, 6fmz, 6fp4 - SmTGR + FAD + piperazine derivative
4la1 - TGR + FAD – Schistosoma japonicum
5w1j, 5w1l - TGR + FAD - Echinococcus granulosus

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Alexander Berchansky, Michal Harel, Marcin Jozef Suskiewicz