EC Number |
Reference |
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1.13.12.5 | free enzyme and in complex with coelenterazine,and mutant K25A/E277A. Diffraction to 1.4 A. Structures demonstrate a classic alpha/beta-hydrolase fold. The presumptive catalytic triad residues are D120, E144, and H285. Additionally determination of structure of the accessory green fluorescent protein |
688385 |
1.13.12.5 | microbatch method is used for crystallization. The crystals of Ca2+-loaded apoaequorin are grown from 0.02 M CaCl2, 30% v/v 2-methyl-2,4-pentanediol, and 0.1 M sodium acetate (pH 4.6) during less than 1 week of incubation at 4°C. The maximum size of crystals is 0.35 * 0.3 * 0.25 mm |
677006 |
1.13.12.5 | molecular docking simulations with the coelenterazine substrate. Two triads of residues are critical for catalysis. Putative catalytic triad residues D120, E144, and H285 bear only limited resemblance to those of aequorin. Residues N53, W121, and P220 are also involved in catalysis |
689921 |
1.13.12.5 | solution structure of fully active, recombinant GLuc. GLuc is an all-alphahelix protein made of nine helices. Two homologous sequential repeats form two anti-parallel bundles made by 4 helices and tied together by three disulfide bonds. The N-terminal helix 1 is grabbed by these 4 helices |
765776 |