Literature summary for 2.4.2.3 extracted from

Lashkov, A.A.; Zhukhlistova, N.E.; Gabdoulkhakov, A.H.; Shtil, A.A.; Efremov, R.G.; Betzel, C.; Mikhailov, A.M.
The X-ray structure of Salmonella typhimurium uridine nucleoside phosphorylase complexed with 2,2-anhydrouridine, phosphate and potassium ions at 1.86 A resolution (2010), Acta Crystallogr. Sect. D, 66, 51-60.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Salmonella enterica subsp. enterica serovar Typhimurium

Crystallization (Commentary)

Crystallization (Comment)	Organism
complexed with 2,2-anhydrouridine, phosphate and potassium ions at 1.86 A resolution. The monomer is an alpha/beta-class polypeptide with a trilayer alpha/beta/alpha sandwich architecture. The potassium ion is located in the intermonomeric region of each homodimer on the local axis of second order of point group 32. The side chains of Glu49B and Ser73B and the carbonyl O atom of Ile69B in the B subunit, as well as symmetrical residues from the D subunit of the BD homodimer, coordinate K+. The residues in the phosphate binding site are Arg30B, Arg91B, Thr94B and Gly26B from the B subunit, and Arg48D from the D subunit	Salmonella enterica subsp. enterica serovar Typhimurium

Crystallization (Comment)

Organism

complexed with 2,2-anhydrouridine, phosphate and potassium ions at 1.86 A resolution. The monomer is an alpha/beta-class polypeptide with a trilayer alpha/beta/alpha sandwich architecture. The potassium ion is located in the intermonomeric region of each homodimer on the local axis of second order of point group 32. The side chains of Glu49B and Ser73B and the carbonyl O atom of Ile69B in the B subunit, as well as symmetrical residues from the D subunit of the BD homodimer, coordinate K+. The residues in the phosphate binding site are Arg30B, Arg91B, Thr94B and Gly26B from the B subunit, and Arg48D from the D subunit

Salmonella enterica subsp. enterica serovar Typhimurium

Organism

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

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Release 2023.1 (January 2023)