29oh | pdb_000029oh

X-ray structure of the adduct formed upon reaction of the gold compound AF-Npx with lysozyme (Structure 1)

spinqualitylabelsall models 29oh, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 29oh is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.54Å Ligands: AU, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LYSC_CHICK Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus. Publication Abstract from PubMed Au(I) complexes are widely investigated as therapeutic agents due to their high affinity for biological nucleophiles and protein targets. Here, the reactivity of an Auranofin (AF) derivative bearing naproxen as a ligand toward hen egg white lysozyme (HEWL) was investigated by a combined crystallographic and computational approach. Notably, the first observation of lysine metalation in HEWL by an Au complex is reported. The results highlight how ligand substitution can significantly affect Au(I) reactivity toward biomacromolecules, enabling noncanonical targeting and potentially impacting biological activity. Tuning Au Reactivity Beyond Canonical Targets: Ligand-Driven Au(I) Metalation of Lysine Residues in Hen Egg White Lysozyme.,Piroddu D, Famlonga L, Tolbatov I, Ferraro G, Chiaverini L, Merlino A, La Mendola D, Marrone A, Marzo T Inorg Chem. 2026 Jul 20;65(28):16296-16304. doi: 10.1021/acs.inorgchem.6c01884. , Epub 2026 Jul 8. PMID:42417613 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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