9i8l

X-ray structure of a polyoxidovanadate/lysozyme adduct obtained when the protein is treated with [VIVO(acac)2] at 310 K

spinqualitylabelsall models 9i8l, resolution 1.83Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9i8l 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 1.831Å Ligands: CL, NA 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 Crystals of the model protein lysozyme were grown and soaked with the potential drug V(IV)O(acetylacetonato)(2) at 37 degrees C. X-ray diffraction and electron paramagnetic resonance (EPR) data collected at this temperature reveal that mixed-valence cage-like polyoxidovanadate clusters are formed and covalently bind protein residue side chains at physiological temperature. Formation of Mixed-Valence Cage-Like Polyoxidovanadates at 37 degrees C Upon Reaction of V(IV)O(acetylacetonato)(2) With Lysozyme.,Tito G, Ferraro G, Garribba E, Merlino A Chemistry. 2025 Apr 24:e202500488. doi: 10.1002/chem.202500488. PMID:40271720 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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