EC Number   |
|---|
    1.1.1.284 | crystal structure of the enzyme in a binary complex with NAD+(gamma) |
| 1.1.1.284 | crystal structures of CBR1 in complex with NADP+ or a substrate mimic (3-(1-tert-butyl-4-amino-1H-indazol-3-yl)phenol) in complex with GSH and the catalytically inert GSH conjugate hydroxymethylglutathione, by vapor diffusion method by growth in the presence of 3-(1-tert-butyl-4-amino-1H-indazol-3-yl)phenol |
| 1.1.1.284 | crystal structures of SlGSNOR apoenzyme, binary complex with NAD+ and a structure crystallized in the presence of NADH and GSH. Catalytic domains of the apoenzyme and of the binary complex with NAD+ are both in the semi-open conformation. The catalytic zinc atoms in the apoenzyme are in a tetrahedral configuration, H-bonded to Cys47, Cys177, His69 and coordinated to the molecule of water in the active site. The coenzyme binding is associated with the catalytic zinc atoms movement towards Glu70 in the catalytic domain in a hydrogen-bonding interaction with the carboxylate oxygen of Glu70. Zinc atoms are in a tetrahedral configuration coordinated with Cys47, Cys177, His69, and Glu70, and they are no longer coordinated with the water molecule. In the SlGSNOR structure crystallized with NADH and GSH, the enzyme appears in closed conformation. Structue analysis, overview |
| 1.1.1.284 | crystals of the binary complex with NAD(H) are grown by a sitting drop vapor diffusion method, where the apoenzyme is equilibrated with a 2 mM NAD+ containing crystallization buffer (0.1 M potassium phosphate, pH 7.1, 12-15% PEG8000, 2 mM DTT, 0.05 mM ZnSO4) |
| 1.1.1.284 | purified recombinant His-tagged enzyme, in complex with NAD+ and with NADH, hanging drop vapour diffusion, mixing of 0.003 ml of 22 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 2.5 mM NAD+, or 2.5 mM NADH and 5.0 mM GSH, 20°C, X-ray diffraction tructure determination and analysis at 1.85-2.14 A resolution, molecular replacement and modeling |
| 1.1.1.284 | sitting-drop vapor diffusion at 4°C. A 15-20 mg/ml enzyme solution equilibrated with a mother liquor containing 0.1 M phosphate buffer, pH 7.1, 10 mM ZnSO4, 1 mM DTT, and 12-16% PEG 8000. Ternary complex with S-(hydroxymethyl)glutathione and the reduced coenzyme to 2.6 A resolution |
| 1.1.1.284 | sitting-drop vapor-diffusion method at 4°C from a 15-20 mg/ml enzyme solution equilibrated with 0.1 M potassium phosphate buffer pH 6.9-7.1, 0.1 mM ZnSO4, 1 mM dithiothreitol, 12-15% PEG8000. Binary complex with substrate 12-hydroxydodecanoic acid and a ternary complex with NAD+ and the inhibitor dodecanoic acid are determined at 2.0 and 2.3 A resolution by X-ray crystallography using the anomalous diffraction signal of zinc |
| 1.1.1.284 | structure of GSNOR1 of both apo- and holoform, to 1.8 A and 2.3 A resolution, respectively |
