Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Crystallization (Commentary)

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 32 > >>
EC Number Crystallization (Commentary) Reference
Show all pathways known for 4.2.1.10Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.10- 5478, 5485, 653902
Show all pathways known for 4.2.1.10Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.103 different crystal forms 649195
Show all pathways known for 4.2.1.10Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.10crystal structure in complex with (2R)-2-methyl-3-dehydroquinic acid, a substrate analogue, at 1.5 A. Residues Gln236, Pro234 and Ala233 are located in the flexible substrate-covering loop. Gln236 is responsible for the folding of this loop and for the dramatic reduction of its flexibility, which triggers active site closure. Glu46 is important in bringing the substrate close to the lysine/histidine catalytic pocket to initiate catalysis 747022
Show all pathways known for 4.2.1.10Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.10crystals obtained in space and on earth using the counter-diffusion technique 649240
Show all pathways known for 4.2.1.10Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.10DHQ2 in complex with (2R)-2-p-methoxybenzyl-3-dehydroquinic acid, sitting drop vapour diffusion method, 20 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 1 mM 2-mercaptoethanol, 1 mM EDTA, and 200 mM NaCl, with addition of (2R)-2-p-methoxybenzyl-3-dehydroquinic acid at 0.25 M in methanol and added at a ratio of 1:20 v/v, mixing of 0.002 ml protein solution with 0.002 ml reservoir solution containing 31% w/v PEG 4000 and 0.1 M sodium citrate, pH 5.0, and equilibation against 0.15 ml reservoir solution, room temperature, X-ray diffraction structure determination and analysis at 2.4-2.5 A resolution, modelling 714749
Show all pathways known for 4.2.1.10Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.10DHQ2 in complex with (2R)-2-p-methoxybenzyl-3-dehydroquinic acid, sitting drop vapour diffusion method, 20 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 1 mM 2-mercaptoethanol, 1 mM EDTA, and 200 mM NaCl, with addition of (2R)-2-p-methoxybenzyl-3-dehydroquinic acid at 0.25 M in methanol and added at a ratio of 1:20 v/v, mixing of 0.002 ml protein solution with 0.002 ml reservoir solution containing 32% v/v 2-methyl-2,4-pentanediol, 0.3 M ammonium sulfate and 0.1 M HEPES, pH 7.5, and equilibation against 0.15 ml reservoir solution, room temperature, X-ray diffraction structure determination and analysis at 2.4-2.5 A resolution, modelling 714749
Show all pathways known for 4.2.1.10Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.10DHQ2 in complex with inhibitors (4R,6R,7S)-4,6,7-trihydroxy-2-[(1Z)-prop-1-en-1-yl]-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid and (4R,6R,7S)-2-(1-cyclopropylethyl)-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid, X-ray diffraction structure determination and analysis at 1.95 and 1.85 A resolution, respectively 714752
Show all pathways known for 4.2.1.10Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.10DHQase-AH9095 complex 677327
Show all pathways known for 4.2.1.10Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.10enzyme in complex with product 3-dehydroshikimate, X-ray diffraction structure determination and analysis 714105
Show all pathways known for 4.2.1.10Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.10hanging drop vapor diffusion method 649154, 651312
Results 1 - 10 of 32 > >>