2a0x Summary

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Structure of human purine nucleoside phosphorylase H257F mutant

The structure was published by Murkin, A.S., Birck, M.R., Rinaldo-Matthis, A., et al., Taylor, E.A., Almo, S.C., and Schramm, V.L., in 2007 in a paper entitled "Neighboring group participation in the transition state of human purine nucleoside phosphorylase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.28 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 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 (CATH) Sequence family (Pfam)
A (P00491) Rossmann foldsearch PF01048: Phosphorylase superfamilysearch

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

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