1K3F

Uridine Phosphorylase from E. coli, Refined in the Monoclinic Crystal Lattice

Summary for 1K3F

• Entry DOI: 10.2210/pdb1k3f/pdb
• Descriptor: uridine phosphorylase (1 entity in total)
• Functional Keywords: nucleoside phosphorylase, hexamer, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P12758
• Total number of polymer chains: 6
• Total formula weight: 163134.33

Authors

Morgunova, E.Yu.,Mikhailov, A.M.,Popov, A.N.,Blagova, E.V.,Smirnova, E.A.,Vainshtein, B.K.,Mao, C.,Armstrong, S.R.,Ealick, S.E.,Komissarov, A.A.,Linkova, E.V.,Burlakova, A.A.,Mironov, A.S.,Debabov, V.G. (deposition date: 2001-10-02, release date: 2001-10-10, Last modification date: 2024-04-03)

Primary citation

Morgunova, E.Yu.,Mikhailov, A.M.,Popov, A.N.,Blagova, E.V.,Smirnova, E.A.,Vainshtein, B.K.,Mao, C.,Armstrong, S.R.,Ealick, S.E.,Komissarov, A.A.,Linkova, E.V.,Burlakova, A.A.,Mironov, A.S.,Debabov, V.G.
Atomic structure at 2.5 A resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice.
FEBS Lett., 367:183-187, 1995

PubMed Abstract: Uridine phosphorylase from E. coli (Upase) has been crystallized using vapor diffusion technique in a new monoclinic crystal form. The structure was determined by the molecular replacement method at 2.5 A resolution. The coordinates of the trigonal crystal form were used as a starting model and the refinement by the program XPLOR led to the R-factor of 18.6%. The amino acid fold of the protein was found to be the same as that in the trigonal crystals. The positions of flexible regions were refined. The conclusion about the involvement in the active site is in good agreement with the results of the biochemical experiments.

PubMed: 7796917
DOI: 10.1016/0014-5793(95)00489-V

Experimental method

X-RAY DIFFRACTION (2.5 Å)