Literature summary for 2.6.1.16 extracted from

Hussein, S.; Kubba, A.; Abdula, A.
Docking study of some new 2, 5-disubstituted-1, 3, 4-thiadiazole derivatives against glucosamine-6-phosphate synthase (2016), Int. J. Appl. Chem., 12, 1-10.

No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment)	Organism
docking 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	Escherichia coli

Crystallization (Comment)

Organism

docking 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

Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
1,1'-[1,3,4-thiadiazole-2,5-diylbis[sulfanediyl(1-oxoethane-2,1-diyl)]]ditetrahydropyridazine-3,6-dione	-	Escherichia coli
2,2'-(1,3,4-thiadiazole-2,5-diyldisulfanediyl)bis[N-(pyrrolidin-1-yl)acetamide]	-	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P17169	-	-

Synonyms

Synonyms	Comment	Organism
GlmS	-	Escherichia coli

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Release 2023.1 (January 2023)