1pwy Summary



The structure was published by dos Santos, D.M., Canduri, F., Pereira, J.H., et al., Basso, L.A., de Azevedo, W.F., and Santos, D.S., in 2003 in a paper entitled "Crystal structure of human purine nucleoside phosphorylase complexed with acyclovir." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 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 Molecular function (GO) Biological process (GO) Cellular component (GO)
E (P00491) purine-nucleoside phosphorylase activitysearch transferase activitysearch purine nucleobase bindingsearch nucleoside bindingsearch drug bindingsearch phosphate ion bindingsearch transferase activity, transferring glycosyl groupssearch catalytic activitysearch transferase activity, transferring pentosyl groupssearch urate biosynthetic processsearch interleukin-2 secretionsearch nicotinamide riboside catabolic processsearch response to drugsearch nucleobase-containing small molecule metabolic processsearch positive regulation of T cell proliferationsearch NAD biosynthesis via nicotinamide riboside salvage pathwaysearch purine nucleobase metabolic processsearch purine nucleotide catabolic processsearch purine-containing compound salvagesearch inosine catabolic processsearch nucleobase-containing compound metabolic processsearch positive regulation of alpha-beta T cell differentiationsearch small molecule metabolic processsearch immune responsesearch nucleoside metabolic processsearch cytoskeletonsearch extracellular vesicular exosomesearch intracellularsearch cytoplasmsearch cytosolsearch

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