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EC Number Crystallization (Commentary) Reference
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16the crystal structure of the C1A mutant of Escherichia coli GlmS, solved at 2.5 A resolution, is organized as a hexamer, where the glutaminase domains adopt an inactive conformation 722779
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16molecular model of the 3-D on the basis of the crystal structures of Escherichia coli GlcN-6-P synthase, PDB entry 4AMV and Candida albicans GlcN-6-P synthase, PDB entry 2POC. The protein has a terminal glutamine amidotransferase type 2 domain (residues 2-318). The phosphosugar-binding SIS domain (residues 390-529; 562-707) plays a key role in catalysis and communication of fructose 6-phosphate and D-glucosamine 6-phosphate between the two active sites 737920
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16molecular docking of inhibitors methyl (2E)-4-([(2S)-2,3-diamino-3-oxopropyl]amino)-4-oxobut-2-enoate and methyl (2E)-4-([(2S)-2-amino-3-(methylamino)-3-oxopropyl]amino)-4-oxobut-2-enoate 738162
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16docking study using inhibitors 1,1'-[1,3,4-thiadiazole-2,5-diylbis[sulfanediyl(1-oxoethane-2,1-diyl)]]ditetrahydropyridazine-3,6-dione, 2,2'-(1,3,4-thiadiazole-2,5-diyldisulfanediyl)bis[N-(pyrrolidin-1-yl)acetamide]. The binding pocket of the enzyme includes the residues, Cys300, Gly301, Thr302, Ser303, Ser347, Gln348, Ser349, Thr352, Val399, Ser401, Ala602 and Lys603. The high docking energies of all generated conformers of 1,1'-[1,3,4-thiadiazole-2,5-diylbis[sulfanediyl(1-oxoethane-2,1-diyl)]]ditetrahydropyridazine-3,6-dione are strongly proportional to the antibacterial activities 738388
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