5V4H

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

Summary for 5V4H

Entry DOI	10.2210/pdb5v4h/pdb
Related	5V4G 5V4I
Descriptor	Lysozyme C, SODIUM ION, PARA-CYMENE RUTHENIUM CHLORIDE, ... (4 entities in total)
Functional Keywords	metal-based, anticancer, ruthenium, lysozyme, hydrolase
Biological source	Gallus gallus (Chicken)
Cellular location	Secreted: P00698
Total number of polymer chains	1
Total formula weight	14660.34
Authors	Sullivan, M.P.,Hartinger, C.G.,Goldstone, D.C. (deposition date: 2017-03-09, release date: 2017-04-05, Last modification date: 2023-10-04)
Primary citation	Sullivan, M.P.,Groessl, M.,Meier, S.M.,Kingston, R.L.,Goldstone, D.C.,Hartinger, C.G. The metalation of hen egg white lysozyme impacts protein stability as shown by ion mobility mass spectrometry, differential scanning calorimetry, and X-ray crystallography. Chem. Commun. (Camb.), 53:4246-4249, 2017 Cited by PubMed Abstract: 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. PubMed: 28361137 DOI: 10.1039/c6cc10150j PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.22 Å)

Structure validation