2Q0M

Tricarbonylmanganese(I)-lysozyme complex : a structurally characterized organometallic protein

Summary for 2Q0M

Entry DOI	10.2210/pdb2q0m/pdb
Descriptor	Lysozyme C, CHLORIDE ION, SODIUM ION, ... (7 entities in total)
Functional Keywords	organometallic protein, tricarbonyl manganese(i), hydrolase
Biological source	Gallus gallus (chicken)
Cellular location	Secreted: P00698
Total number of polymer chains	1
Total formula weight	14678.65
Authors	Razavet, M.,Artero, V.,Cavazza, C.,Oudart, Y.,Fontecilla-Camps, J.C.,Fontecave, M. (deposition date: 2007-05-22, release date: 2007-12-11, Last modification date: 2024-10-30)
Primary citation	Razavet, M.,Artero, V.,Cavazza, C.,Oudart, Y.,Lebrun, C.,Fontecilla-Camps, J.C.,Fontecave, M. Tricarbonylmanganese(I)-lysozyme complex: a structurally characterized organometallic protein. Chem.Commun.(Camb.), :2805-2807, 2007 Cited by PubMed Abstract: The reaction of the new and structurally characterized covalent {Mn(CO)(3)(H(2)O)(2)}(+)-lysozyme adduct with NiS(4) and NiN(2)S(2) complexes generates binuclear Ni-Mn complexes; relevance to the reactivity of the protein-bound {Fe(CO)(CN)(2)} intermediate during maturation of [NiFe] hydrogenases is discussed. PubMed: 17609782 DOI: 10.1039/b703887a PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation