Literature summary for 1.8.1.B1 extracted from

Huang, J.; Hua, W.; Li, J.; Hua, Z.
Molecular docking to explore the possible binding mode of potential inhibitors of thioredoxin glutathione reductase (2015), Mol. Med. Rep., 12, 5787-5795 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular docking of inhibitory compounds into the NADPH binding site, the active site of the thioredoxin reductase domain and the glutaredoxin active site. The most favoured binding site for all compounds is the oxidized glutathione-binding pocket of the thioredoxin reductase domain	Schistosoma japonicum
molecular docking of inhibitory compounds into the NADPH binding site, the active site of the thioredoxin reductase domain and the glutaredoxin active site. The most favoured binding site for all compounds is the oxidized glutathione-binding pocket of the thioredoxin reductase domain. Peptide fragments Phe505'-Leu508' and Pro572'-Thr577' play a critical role in the interactions with the inhibitors	Schistosoma mansoni

Crystallization (Comment)

Organism

molecular docking of inhibitory compounds into the NADPH binding site, the active site of the thioredoxin reductase domain and the glutaredoxin active site. The most favoured binding site for all compounds is the oxidized glutathione-binding pocket of the thioredoxin reductase domain

Schistosoma japonicum

Schistosoma mansoni

Organism

Organism	UniProt	Comment	Textmining
Schistosoma japonicum	B5THG7	-	-
Schistosoma mansoni	Q962Y6	-	-

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Release 2023.1 (January 2023)