4QGZ
X-ray structure of the adduct formed between hen egg white lysozyme and trans-dimethylamine methylamine dichlorido platinum(II)
Summary for 4QGZ
Entry DOI | 10.2210/pdb4qgz/pdb |
Related | 2I6Z 4J1A 4J1B 4LFK 4LFP 4LGK 4MR1 4NY5 4QH3 |
Descriptor | Lysozyme C, bis(chloranyl)-(dimethylamino)-(methylamino)platinum (3 entities in total) |
Functional Keywords | lysozyme fold, hydrolase, o-glycosyl hydrolase |
Biological source | Gallus gallus (bantam,chickens) |
Cellular location | Secreted: P00698 |
Total number of polymer chains | 1 |
Total formula weight | 15011.38 |
Authors | Russo Krauss, I.,Merlino, A. (deposition date: 2014-05-26, release date: 2014-07-30, Last modification date: 2014-08-20) |
Primary citation | Messori, L.,Marzo, T.,Michelucci, E.,Russo Krauss, I.,Navarro-Ranninger, C.,Quiroga, A.G.,Merlino, A. Interactions between Anticancer trans-Platinum Compounds and Proteins: Crystal Structures and ESI-MS Spectra of Two Protein Adducts of trans-(Dimethylamino)(methylamino)dichloridoplatinum(II). Inorg.Chem., 53:7806-7808, 2014 Cited by PubMed Abstract: The adducts formed between trans-(dimethylamino)(methylamino)dichloridoplatinum(II), [t-PtCl2(dma)(ma)], and two model proteins, i.e., hen egg white lysozyme and bovine pancreatic ribonuclease, were independently characterized by X-ray crystallography and electrospray ionization mass spectrometry. In these adducts, the Pt(II) center, upon chloride release, coordinates either to histidine or aspartic acid residues while both alkylamino ligands remain bound to the metal. Comparison with the cisplatin derivatives of the same proteins highlights for [t-PtCl2(dma)(ma)] a kind of biomolecular metalation remarkably different from that of cisplatin. PubMed: 25025479DOI: 10.1021/ic5012583 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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