3QNG

Crystal Structure Analysis of Lysozyme-bound fac-[Re(CO)3(L-serine)]

Summary for 3QNG

Entry DOI	10.2210/pdb3qng/pdb
Related	3QE8
Descriptor	Lysozyme C, Tricarbonyl (L-serine) rhenium(I), CHLORIDE ION, ... (6 entities in total)
Functional Keywords	hydrolase, rhenium complex, metallation
Biological source	Gallus gallus (Chicken)
Cellular location	Secreted: P00698
Total number of polymer chains	1
Total formula weight	14825.99
Authors	Zobi, F.,Spingler, B. (deposition date: 2011-02-08, release date: 2012-01-18, Last modification date: 2024-11-20)
Primary citation	Zobi, F.,Spingler, B. Post-protein-binding reactivity and modifications of the fac-[Re(CO)3]+ core Inorg.Chem., 51:1210-1212, 2012 Cited by PubMed Abstract: The reactivity of the [Re(CO)(3)(H(2)O)(2)](+) complex coordinated to the His15 residue of HEW lysozyme is described. In the fully metalated protein (Lys-1), the Re ion retains its reactivity only toward selected ligands, while others induce a ligand-mediated demetalation of the enzyme. It is further shown that some of the complexes that may be "engineered" on the lysozyme do not react with the free protein even if present in solution in excess. The formation of stable metal adducts starting from Lys-1 was confirmed by X-ray crystallography. PubMed: 22229733 DOI: 10.1021/ic2023314 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.55 Å)

Structure validation