1m73 Summary

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CRYSTAL STRUCTURE OF HUMAN PNP AT 2.3A RESOLUTION

The structure was published by de Azevedo, W.F., Canduri, F., dos Santos, D.M., et al., Mendes, M.A., Palma, M.S., and Santos, D.S., in 2003 in a paper entitled "Crystal structure of human purine nucleoside phosphorylase at 2.3A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2002.

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

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