7ti1

Structure of AmpC bound to RPX-7063 at 2.0A

spinqualitylabelsall models 7ti1, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ti1 is a 1 chain structure with sequence from Enterobacter cloacae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: CL, EDO, ZXQ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AMPC_ENTCL This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. Publication Abstract from PubMed Early efforts to broaden the spectrum and potency of cyclic boronic acid beta-lactamase inhibitor vaborbactam included a series of 7-membered ring boronates. Exploration of stereoisomers and incorporation of heteroatoms allowed identification of the all-carbon cyclic boronate with substituents trans as the preferred core structure, showing inhibition of Class A and C enzymes. Crystal structures of one analog bound to important beta-lactamase enzymes were obtained. When isolated under acidic conditions, these compounds spontaneously formed a neutral cyclic anhydride (intramolecular prodrug) which was shown to have much-improved oral bioavailability (52-69%) compared to the ring-opened carboxylate salt (9%). Broad-spectrum cyclic boronate beta-lactamase inhibitors featuring an intramolecular prodrug for oral bioavailability.,Raja Reddy K, Totrov M, Lomovskaya O, Griffith DC, Tarazi Z, Clifton MC, Hecker SJ Bioorg Med Chem. 2022 May 15;62:116722. doi: 10.1016/j.bmc.2022.116722. Epub 2022, Mar 23. PMID:35358864 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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