1rfg Summary

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Crystal Structure of Human Purine Nucleoside Phosphorylase Complexed with Guanosine

The structure was published by Canduri, F., Silva, R.G., dos Santos, D.M., et al., Basso, L.A., Santos, D.S., and de Azevedo, W.F., in 2005 in a paper entitled "Structure of human PNP complexed with ligands." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.9 Å and deposited in 2003.

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 288 residues which is 100% of the natural sequence. Out of 288 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
E Purine nucleoside phosphorylase P00491 (2-289) (PNPH_HUMAN)search Homo sapienssearch 100% 288 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00491 (2 - 289) Purine nucleoside phosphorylase Homo sapiens

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

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

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