3FWP

X-ray structure of uridine nucleoside phosphorylease from Salmonella typhimurium complexed with phosphate and its inhibitor 2,2'-anhydrouridine at 1.86 A resolution

Summary for 3FWP

• Entry DOI: 10.2210/pdb3fwp/pdb
• Descriptor: Uridine phosphorylase, PHOSPHATE ION, POTASSIUM ION, ... (5 entities in total)
• Functional Keywords: cytoplasm, glycosyltransferase, transferase
• Biological source: Salmonella typhimurium
• Cellular location: Cytoplasm : P0A1F6
• Total number of polymer chains: 6
• Total formula weight: 164095.32

Authors

Lashkov, S.A.,Mikhailov, A.M.,Gabdulkhakov, A.G. (deposition date: 2009-01-19, release date: 2010-01-19, Last modification date: 2023-09-06)

Primary citation

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.
Acta Crystallogr.,Sect.D, 66:51-60, 2010

PubMed Abstract: Uridine nucleoside phosphorylase is an important drug target for the development of anti-infective and antitumour agents. The X-ray crystal structure of Salmonella typhimurium uridine nucleoside phosphorylase (StUPh) complexed with its inhibitor 2,2'-anhydrouridine, phosphate and potassium ions has been solved and refined at 1.86 A resolution (R(cryst) = 17.6%, R(free) = 20.6%). The complex of human uridine phosphorylase I (HUPhI) with 2,2'-anhydrouridine was modelled using a computational approach. The model allowed the identification of atomic groups in 2,2'-anhydrouridine that might improve the interaction of future inhibitors with StUPh and HUPhI.

PubMed: 20057049
DOI: 10.1107/S0907444909044175

Experimental method

X-RAY DIFFRACTION (1.86 Å)