EC Number |
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3.5.4.4 | - |
3.5.4.4 | commercial enzyme preparation at 20 mg/ml, native enzyme or complexed with inhibitor purine riboside, sitting drop vapour diffusion method, micro-stirring technique over 2 weeks, from 2.2 M ammonium sulfate, 2% 2-methyl-2,4-pentanediol, 0.1 M MES, pH 6.0, 20°C, with reservoir solution containing 20% 2-propanol, 20% PEG 4000, 0.1 M citrate, pH 5.6, X-ray diffraction structure determination and analysis at 1.8 A resolution |
3.5.4.4 | crystal structure of a surface engineered adenosine deaminase at a resolution of 2.48 A |
3.5.4.4 | crystal structure of adenosine deaminase from Plasmodium vivax in complex with inhibitor, 2-deoxycoformycin (pentostatin), 33% PEG 20000, 0.1 M TAPS (pH 9.0), 0.1 M Sodium phosphate (monobasic), 16% acetonitrile, 5 mM adenosine, pH 7.0, vapor diffusion, sitting drop, temperature 298K, space group C 2 2 21, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular modeling, crystal structure of adenosine deaminase from Plasmodium vivax in complex with adenosine, space group C 2 2 21, X-ray diffraction structure determination and analysis at 1.89 A resolution, crystal structure of adenosine deaminase from Plasmodium vivax in complex with guanosine, 27.3% PEG 20000, 0.1 M CHES (pH 9.5), 0.1 M Sodium phosphate monobasic, 5 mM guanosine, vapor diffusion, sitting drop, temperature 293K, space group C 2 2 21, X-ray diffraction structure determination and analysis at 2.19 A resolution, these structures highlight a drastic conformational change in plasmodial adenosine deaminase upon substrate binding, these complexes illuminate the structural basis for the differential substrate specificity and potential drug selectivity between mammalian and parasite enzymes |
3.5.4.4 | crystal structure of adenosine deaminase ligated with (+)-erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA), vapor diffusion, sitting drop, 2 M ammonium sulfate, 2% 2-methyl-2, 4-pentanediol, 0.1 M MES buffer, pH 6.0, temperature 293K, , X-ray diffraction structure determination and analysis at 2.52 A resolution, space group P 43 21 2, EHNA induces conformational change of adenosine deaminase to the open form in the crystalline state, structural comparison between the EHNA-ADA complex and the 1-eaza-adenosine-ADA complex |
3.5.4.4 | crystals of the complex of adenosine deaminase with 6-hydroxy-1,6-dihydropurine riboside are grown against reservoirs containing 2.0-2.2 M ammonium sulfate, 2% v/v polyethylene glycol 400 in 0.1 M HEPES buffer, pH 7.5, solved at 2.5 A resolution |
3.5.4.4 | holo- and apo-ADA, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 200 mM ammonium sulfate, pH 4.7 for apo-ADA or 25% (w/v) PEG 6000, 20 mM Tris-HCl and pH 8.5 for holo-ADA |
3.5.4.4 | molecular modeling enzyme-inhibitor, docking simulations enzyme-inhibitor, drug design |
3.5.4.4 | Plasmodium vivax ADA in a complex with 5'-methylthiocoformycin is crystallized by the sitting drop vapor diffusion method, using 25% (w/v) PEG3350, 100 mM HEPES (pH 7.5), and 0.2 M MgCl2 |
3.5.4.4 | purified intestinal enzyme complexed with 1-[(R)-1-hydroxy-4-(6-(5-phenylvalerylamino)indol-1-yl)2-butyl]imidazole-4-carboxamide, 1-[(R)-1-hydroxy-4-(6-(3-phenylpropionylamino)indol-1-yl)2-butyl]imidazole-4-carboxamide, or 1-[(R)-4-(6-(3-benzylureido)indol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide, protein solution is mixed with precipitant solution containing 100 mM MES, pH 6.0, 2.1 ammonium sulfate, and 2.5% v/v PEG 400, X-ray diffraction structure determination and analysis at 2.2 A resolution |