1pf7 Summary

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CRYSTAL STRUCTURE OF HUMAN PNP COMPLEXED WITH IMMUCILLIN H

The structure was published by De Azevedo Jr., W.F., Canduri, F., Dos Santos, D.M., et al., Palma, M.S., Basso, L.A., and Santos, D.S., in 2003 in a paper entitled "Structural basis for inhibition of human PNP by immucillin-H" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 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 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 (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 Biological process (GO) Cellular component (GO) Molecular function (GO)
E (P00491) small molecule metabolic processsearch nucleobase-containing compound metabolic processsearch nicotinamide riboside catabolic processsearch purine nucleobase metabolic processsearch urate biosynthetic processsearch positive regulation of T cell proliferationsearch positive regulation of alpha-beta T cell differentiationsearch interleukin-2 secretionsearch immune responsesearch response to drugsearch inosine catabolic processsearch nucleobase-containing small molecule metabolic processsearch purine nucleotide catabolic processsearch purine-containing compound salvagesearch NAD biosynthesis via nicotinamide riboside salvage pathwaysearch nucleoside metabolic processsearch cytoskeletonsearch cytosolsearch extracellular vesicular exosomesearch cytoplasmsearch intracellularsearch phosphate ion bindingsearch transferase activity, transferring glycosyl groupssearch purine-nucleoside phosphorylase activitysearch drug bindingsearch transferase activitysearch purine nucleobase bindingsearch transferase activity, transferring pentosyl groupssearch nucleoside bindingsearch catalytic activitysearch

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