9qny | pdb_00009qny

APH(2)-Id with a fragment

spinqualitylabelsall models 9qny, resolution 2.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9qny is a 2 chain structure with sequence from Enterococcus casseliflavus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.41Å Ligands: A1I78, DMS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O68183_ENTCA Publication Abstract from PubMed According to the World Health Organization (WHO), antimicrobial resistance is a serious global health issue. Overcoming antibiotic resistance involves several strategies, including the inhibition of resistance mechanisms. Among the various resistance mechanisms, aminoglycoside phosphotransferases (APHs) catalyze the transfer of the gamma-phosphate from a nucleotide donor to various aminoglycosides, leading to their inactivation. In this work, using a fragment-based drug design (FBDD) approach, we have identified and characterized a promising APH inhibitor capable of increasing the sensitivity of Pseudomonas aeruginosa and Staphylococcus aureus resistant to aminoglycosides. It is therefore a good candidate for the future development of APH inhibitors to be prescribed in combination with aminoglycosides. This molecule is a competitive inhibitor of adenosine 5'-triphosphate (ATP), the phosphate donor of APHs. Further studies are required to optimize this molecule to improve its specificity for APHs and its bioavailability in bacteria. Fragment-based drug design of a bacterial kinase inhibitor capable of increasing the antibiotic sensitivity of clinical isolates.,Kowalewski J, Deutscher R, Richardoz M, Tomaszczyk M, Gelin M, Labesse G, Hausch F, Wright GD, Dunyach-Remy C, Guichou JF, Lionne C Commun Chem. 2025 Nov 27;8(1):417. doi: 10.1038/s42004-025-01795-6. PMID:41310159 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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