2a0x Summary


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

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