5v4h | pdb_00005v4h

Ruthenium(II)(cymene)(chlorido)2-lysozyme adduct formed when ruthenium(II)(cymene)(bromido)2 underwent ligand exchange, resulting in one binding site

spinqualitylabelsall models 5v4h, resolution 1.22Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5v4h 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 1.22Å Ligands: NA, RU7 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 Metalation of hen egg white lysozyme (HEWL) with organometallics was studied with physicochemical methods in solid state, solution and the gas phase. While metalation did not affect the crystal structure of HEWL significantly, protein destabilisation was detected in gas phase and solution. The metalation of hen egg white lysozyme impacts protein stability as shown by ion mobility mass spectrometry, differential scanning calorimetry, and X-ray crystallography.,Sullivan MP, Groessl M, Meier SM, Kingston RL, Goldstone DC, Hartinger CG Chem Commun (Camb). 2017 Apr 11;53(30):4246-4249. doi: 10.1039/c6cc10150j. PMID:28361137 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lysozyme 3D structures

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