1ula Summary

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PDB entry 1ula (supersedes 2pnp)

APPLICATION OF CRYSTALLOGRAPHIC AND MODELING METHODS IN THE DESIGN OF PURINE NUCLEOSIDE PHOSPHORYLASE INHIBITORS

The structure was published by Ealick, S.E., Babu, Y.S., Bugg, C.E., et al., Guida, W.C., Montgomery, J.A., and Secrist 3rd., J.A., in 1991 in a paper entitled "Application of crystallographic and modeling methods in the design of purine nucleoside phosphorylase inhibitors." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.75 Å and deposited in 1991.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of PURINE NUCLEOSIDE PHOSPHORYLASE. This molecule has the UniProt identifier P00491 (PNPH_HUMAN)search. The sample contained 289 residues which is 100% of the natural sequence. Out of 289 residues 288 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotrimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PURINE NUCLEOSIDE PHOSPHORYLASE P00491 (1-289) (PNPH_HUMAN)search Homo sapienssearch 100% 289 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00491 (1 - 289) PURINE NUCLEOSIDE PHOSPHORYLASE Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00491) Purine and uridine phosphorylasessearch Rossmann foldsearch PF01048: Phosphorylase superfamilysearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P00491) catalytic activitysearch purine-nucleoside phosphorylase activitysearch drug bindingsearch transferase activitysearch phosphate ion bindingsearch nucleoside bindingsearch transferase activity, transferring glycosyl groupssearch purine nucleobase bindingsearch transferase activity, transferring pentosyl groupssearch nucleoside metabolic processsearch purine nucleotide catabolic processsearch response to drugsearch purine nucleobase metabolic processsearch nicotinamide riboside catabolic processsearch urate biosynthetic processsearch immune responsesearch inosine catabolic processsearch positive regulation of T cell proliferationsearch purine-containing compound salvagesearch small molecule metabolic processsearch interleukin-2 secretionsearch NAD biosynthesis via nicotinamide riboside salvage pathwaysearch positive regulation of alpha-beta T cell differentiationsearch nucleobase-containing small molecule metabolic processsearch nucleobase-containing compound metabolic processsearch extracellular vesicular exosomesearch cytoplasmsearch cytosolsearch cytoskeletonsearch intracellularsearch

Chain InterPro annotation
A Nucleoside phosphorylase domainsearch PNP/MTAP phosphorylasesearch Purine nucleoside phosphorylasesearch Purine nucleoside phosphorylase I, inosine/guanosine-specificsearch Purine phosphorylase, family 2, conserved sitesearch