1rr6 Summary

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Structure of human purine nucleoside phosphorylase in complex with Immucillin-H and phosphate

The structure was published by Shi, W., Ting, L.M., Kicska, G.A., et al., Kim, K., Almo, S.C., and Schramm, V.L., in 2004 in a paper entitled "Plasmodium falciparum purine nucleoside phosphorylase: crystal structures, immucillin inhibitors, and dual catalytic function." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 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 289 residues which is 100% of the natural sequence. Out of 289 residues 282 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 97%


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

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