Literature summary extracted from

Lashkov, A.; Zhukhlistova, N.; Sotnichenko, S.; Gabdulkhakov, A.; Mikhailov, A.
Structural basis for the mechanism of inhibition of uridine phosphorylase from Salmonella typhimurium (2010), Crystallogr. Rep., 55, 41-57.

No PubMed abstract available

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
2.4.2.3	expression in Escherichia coli	Salmonella enterica subsp. enterica serovar Typhimurium

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.4.2.3	in complex with with the inhibitor 2,2'-anhydrouridine, the substrate phosphate, and with both the inhibitor 2,2'-anhydrouridine and the substrate phosphate, to 2.38, 1.5 and 1.75 A resolution, respectively. The presence of the phosphate ion in the phosphate-binding site substantially changes the orientations of the side chains of the amino-acid residues Arg30, Arg91, and Arg48 coordinated to this ion. The highly flexible loop L9 is unstable	Salmonella enterica subsp. enterica serovar Typhimurium

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.4.2.3	Salmonella enterica subsp. enterica serovar Typhimurium	P0A1F6	-	-

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Release 2023.1 (January 2023)