EC Number   |
|---|
   1.8.1.B1 | crystal structure at 2.2 A resolution of TGR, deleted in the last two residues |
| 1.8.1.B1 | crystallization of the enzyme in complex with 1,8-naphthyridine-2 carboxylate and with the 1-(2-hydroxyethyl)piperazine derivatives, sitting drop vapor diffusion method |
| 1.8.1.B1 | in complex with FAD, orthorhombic space group P212121, with unit-cell parameters a 84.185, b 86.47, c 183.164 A |
| 1.8.1.B1 | modeled structure is a functional dimer, and contains a Grx domain (residues 2183), a FAD/NADPH-binding domain or TrxR domain (residues 109450) and a dimerization domain (residues 470598) |
| 1.8.1.B1 | 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 |
| 1.8.1.B1 | 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 |
| 1.8.1.B1 | sitting drop method |
| 1.8.1.B1 | to 2.7 A resolution, space group of P43212, one physiological homodimer per asymmetric unit. Structure displays distinct binding sites for thioredoxin and the glutaredoxin domain, a single glutathione disulfide reduction site in the Grx domain, and rotation of the glutaredoxin domain toward the Sec-containing redox active site |
