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Results 1 - 10 of 17 > >>
EC Number Crystallization (Commentary) Reference
Show all pathways known for 2.5.1.15Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.15- 663405, 759244
Show all pathways known for 2.5.1.15Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.15a complex of the purified bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/dihydropteroate synthase with a pterin monophosphate substrate analogue, structure solved by molecular replacement and refined to 2.3 A resolution 662648
Show all pathways known for 2.5.1.15Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.15an inhibitor is soaked into the apo crystals of the enzyme and the structure of the complex is determined to 2.1 A resolution. Thed inhibitor occupies both the pterin and 4-aminobenzoate binding pocket of the enzyme 758913
Show all pathways known for 2.5.1.15Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.15apo-enzyme, and enzyme in complex with HPPK substrate 6-hydroxymethyl-7,8-dihydropterin or inhibitor 2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydorpyrimido[4,5-c]pyridazin-3-yl)propanoic acid, X-ray diffraction structure determination and analysis at 2.2-2.3 A resolution 723522
Show all pathways known for 2.5.1.15Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.15apo-structure and structure of the complex with pteroate, analysis, overview 723771
Show all pathways known for 2.5.1.15Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.15apoenzyme (PDB: 2VEF), complex with 6-hydroxymethyl-7,8-dihydropterin monophosphate (DHPP) (PDB: 2VEG), TIM alpha/beta barrel fold with highly conserved 6-hydroxymethyl-7,8-dihydropterin diphosphate-binding pocket, crystals: space group P2(1)2(1)2(1), unit cell parameters: a: 45, b: 90, c: 137, loop 1 and 2 highly flexible, dimer of two identical monomers in the asymmetric unit, in complex with DHPP only one monomer of the dimer has substrate bound wide-scale rearrangement of active site upon 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPPP) binding mediated by diphosphate moiety, hanging-drop method: 2 microlitre protein solution (13 mg/ml) + 2 microl precipitant (0.2 M ammonium iodide, 20% (w/v) poly(ethylene glycol) 3350) +/-2.5 mM DHPPP (hydrolysis to DHPP during crystallization), 7-14 days, molecular replacement-based structure determination 690820
Show all pathways known for 2.5.1.15Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.15hanging-drop vapor-diffusion method at 20°C, crystal structure of the enzyme in complex with four substrates/analogs 759490
Show all pathways known for 2.5.1.15Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.15HPPK-DHPS from wild type and sulfa-resistant parasites, in complex with pteroate, sulfathiazole-dihydropteroate, and sulfadoxine-dihydropteroate, microbatch method, using 0.1 mM bicine pH 9.0, 0.5-0.6 M calcium acetate-Ca(OAc)2, 20% (w/v) PEG 4000 at 25°C 759184
Show all pathways known for 2.5.1.15Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.15in complex with 6-hydroxymethylpterin diphosphate, pterin, the ATP analog AMPCPP, and 4-aminobenzoate, at 20°C, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M potassium citrate tribasic monohydrate 759490
Show all pathways known for 2.5.1.15Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.15in complex with inhibitors 759069
Results 1 - 10 of 17 > >>