1v3q Summary


Structure of human PNP complexed with DDI

The structure was published by Canduri, F., dos Santos, D.M., Silva, R.G., et al., Palma, M.S., de Azevedo Jr., W.F., and Santos, D.S., in 2004 in a paper entitled "Structures of human purine nucleoside phosphorylase complexed with inosine and ddI" (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) Cellular component (GO) Biological process (GO)
E (P00491) nucleoside bindingsearch purine nucleobase bindingsearch catalytic activitysearch purine-nucleoside phosphorylase activitysearch drug bindingsearch transferase activitysearch transferase activity, transferring glycosyl groupssearch transferase activity, transferring pentosyl groupssearch phosphate ion bindingsearch intracellularsearch cytoplasmsearch cytosolsearch cytoskeletonsearch extracellular vesicular exosomesearch nucleobase-containing compound metabolic processsearch purine nucleobase metabolic processsearch inosine catabolic processsearch purine nucleotide catabolic processsearch nicotinamide riboside catabolic processsearch immune responsesearch nucleoside metabolic processsearch NAD biosynthesis via nicotinamide riboside salvage pathwaysearch urate biosynthetic processsearch positive regulation of T cell proliferationsearch response to drugsearch purine-containing compound salvagesearch small molecule metabolic processsearch positive regulation of alpha-beta T cell differentiationsearch nucleobase-containing small molecule metabolic processsearch interleukin-2 secretionsearch

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