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Results 1 - 10 of 31 > >>
EC Number Crystallization (Commentary) Reference
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3- 638516
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3complexed with 2,2-anhydrouridine, phosphate and potassium ions at 1.86 A resolution. The monomer is an alpha/beta-class polypeptide with a trilayer alpha/beta/alpha sandwich architecture. The potassium ion is located in the intermonomeric region of each homodimer on the local axis of second order of point group 32. The side chains of Glu49B and Ser73B and the carbonyl O atom of Ile69B in the B subunit, as well as symmetrical residues from the D subunit of the BD homodimer, coordinate K+. The residues in the phosphate binding site are Arg30B, Arg91B, Thr94B and Gly26B from the B subunit, and Arg48D from the D subunit 721153
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3enzyme in complex with 5-fluorouracil, hanging-drop vapour-diffusion method, 0.5 ml of reservoir solution containing 0.34 ml 0.1 M Tris-maleate/NaOH buffer, pH 5.5, and 0.16 ml 40% w/v PEG 3350 is mixed with 2 ml protein solution containing 11.3 mg/ml enzyme in 10 mM Tris-HCl buffer, pH 7.3, 0.002 ml H2O, 0.0013 ml reservoir solution, 0.002 ml 100 mM 5-fluorouracil, and 0.0003 ml 2-propanol, 21°C, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.2 A resolution, modeling 701526
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3free enzyme and enzyme in complex with inhibitor 5-benzylacyclouridine, 3 mg/ml protein in absence or presence of 1 mM inhibitor from 17% PEG 3350, 100 mM Bis-Tris buffer, pH 5.5, 300 mM KCl, and 30 mM MgCl2, or for the ligand-free enzyme crystals from 1.2 M (NH4)2SO4, 100 mM Bis-Tris buffer pH 5.5, with 1-2% MPD, with 2-3 mg/ml protein, X-ray diffraction structure determination and analysis at 2.3 A and 1.9 A resolution, respectively 702929
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3free enzyme and in complex with uridine, hanging drop vapor diffusion method, using 0.75 M ammonium sulfate, 0.075 M bis-Tris pH 5.5, 0.75% (w/v) PEG 3350, and 25% (v/v) glycerol 735369
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3free isoform UPa and in complex with thymidine, uracil, thymine or 5-fluorouracil, sitting drop vapor diffusion method, using 100 mM trisodium citrate pH5.6, 16% (w/v) PEG4000 and 17.5% (v/v) isopropanol or 100 mM bis-Tris pH 5.5, 25% (w/v) PEG3350 and 200 mM ammonium sulfate 735728
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3free selenomethionine-labeled enzyme, or enzyme in complex with uridine, X-ray diffraction structure determination and analysis at 2.7 A and 1.44 A resolution, respectively 705176
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3hanging drop vapor diffusion method 638519
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3hanging drop vapour-diffusion method, 2.5 A resolution 657483
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3hanging-drop vapour-diffusion method with PEG as precipitant, 2.9 A resolution 657467
Results 1 - 10 of 31 > >>