3g0y | pdb_00003g0y

Structure of E. coli FabF(C163Q) in complex with dihydroplatensimycin

spinqualitylabelsall models 3g0y, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3g0y is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: P9A Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FABF_ECOLI Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Platensimycin (1) displays antibacterial activity due to its inhibition of the elongation condensing enzyme (FabF), a novel mode of action that could potentially lead to a breakthrough in developing a new generation of antibiotics. The medicinal chemistry efforts were focused on the modification of the enone moiety of platensimycin and several analogs showed significant activity against FabF and possess antibacterial activity. Synthesis and biological evaluation of platensimycin analogs.,Shen HC, Ding FX, Singh SB, Parthasarathy G, Soisson SM, Ha SN, Chen X, Kodali S, Wang J, Dorso K, Tata JR, Hammond ML, Maccoss M, Colletti SL Bioorg Med Chem Lett. 2009 Mar 15;19(6):1623-7. Epub 2009 Feb 7. PMID:19233644 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acyl carrier protein synthase 3D structures

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