1m1n | pdb_00001m1n

Nitrogenase MoFe protein from Azotobacter vinelandii

spinqualitylabelsall models 1m1n, resolution 1.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1m1n is a 8 chain structure with sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CFN, CLF, HCA Related: 3min, 2min, 1n2c Activity: Nitrogenase, with EC number 1.18.6.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed A high-resolution crystallographic analysis of the nitrogenase MoFe-protein reveals a previously unrecognized ligand coordinated to six iron atoms in the center of the catalytically essential FeMo-cofactor. The electron density for this ligand is masked in structures with resolutions lower than 1.55 angstroms, owing to Fourier series termination ripples from the surrounding iron and sulfur atoms in the cofactor. The central atom completes an approximate tetrahedral coordination for the six iron atoms, instead of the trigonal coordination proposed on the basis of lower resolution structures. The crystallographic refinement at 1.16 angstrom resolution is consistent with this newly detected component being a light element, most plausibly nitrogen. The presence of a nitrogen atom in the cofactor would have important implications for the mechanism of dinitrogen reduction by nitrogenase. Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor.,Einsle O, Tezcan FA, Andrade SL, Schmid B, Yoshida M, Howard JB, Rees DC Science. 2002 Sep 6;297(5587):1696-700. PMID:12215645 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nitrogenase

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