1yry Summary


Crystal structure of human PNP complexed with MESG

The structure was published by Silva, R.G., Pereira, J.H., Canduri, F., de Azevedo Jr., W.F., Basso, L.A., and Santos, D.S., in 2005 in a paper entitled "Kinetics and crystal structure of human purine nucleoside phosphorylase in complex with 7-methyl-6-thio-guanosine" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 2005.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 (1-289) (PNPH_HUMAN)search Homo sapienssearch 100% 289 99%

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