3ENZ
Arsenolytic structure of Plasmodium falciparum purine nucleoside phosphorylase with hypoxanthine, ribose and arsenate ion
Summary for 3ENZ
| Entry DOI | 10.2210/pdb3enz/pdb |
| Descriptor | Purine nucleoside phosphorylase, HYPOXANTHINE, 1,4-anhydro-D-ribitol, ... (7 entities in total) |
| Functional Keywords | transferase, catalytically-relevant arsenolytic-intermediate-state complex, glycosyltransferase |
| Biological source | Plasmodium falciparum |
| Total number of polymer chains | 6 |
| Total formula weight | 171448.38 |
| Authors | Chaikuad, A.,Brady, R.L. (deposition date: 2008-09-26, release date: 2009-08-04, Last modification date: 2023-09-06) |
| Primary citation | Chaikuad, A.,Brady, R.L. Conservation of structure and activity in Plasmodium purine nucleoside phosphorylases. Bmc Struct.Biol., 9:42-42, 2009 Cited by PubMed Abstract: Purine nucleoside phosphorylase (PNP) is central to purine salvage mechanisms in Plasmodium parasites, the causative agents of malaria. Most human malaria results from infection either by Plasmodium falciparum (Pf), the deadliest form of the parasite, or by the widespread Plasmodium vivax (Pv). Whereas the PNP enzyme from Pf has previously been studied in detail, despite the prevalence of Pv little is known about many of the key metabolic enzymes from this parasite, including PvPNP. PubMed: 19575810DOI: 10.1186/1472-6807-9-42 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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