1vfn
PURINE NUCLEOSIDE PHOSPHORYLASE
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OverviewOverview
Trimeric calf spleen purine nucleoside phosphorylase has been complexed, with hypoxanthine via phosphorolysis of inosine in the presence of, phosphate. The resulting, "Michaelis" complex (three hypoxanthine, molecules per trimer), presumed to be formed under these conditions, crystallized in the cubic space group P2(1)3, with unit cell dimension a =, 94.11 A and one monomer in the asymmetric crystal unit; the biologically, active trimer is located on the crystallographic 3-fold axis., High-resolution X-ray diffraction data were collected using synchrotron, radiation (EMBL outstation, Hamburg, c/o DESY). The crystal structure has, been determined by molecular replacement and refined at 2.15 A resolution, to an R-value of 0.18. In the hypoxanthine binding site, a cis-peptide, bond between ... [(full description)]
About this StructureAbout this Structure
1VFN is a [Single protein] structure of sequence from [Bos taurus] with MG, ZN and HPA as [ligands]. Active as [Purine-nucleoside phosphorylase], with EC number [2.4.2.1]. Structure known Active Sites: BAS and PRE. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15 A resolution., Koellner G, Luic M, Shugar D, Saenger W, Bzowska A, J Mol Biol. 1997 Jan 17;265(2):202-16. PMID:9020983
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