3efu | pdb_00003efu

X-ray structure of human ubiquitin-Hg(II) adduct

spinqualitylabelsall models 3efu, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3efu is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HG Related: 1ubq Gene: RPS27A, UBA80, UBCEP1, UBA52, UBCEP2, UBB, UBC (Homo sapiens) 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 structural investigation performed on adducts of human ubiquitin with group-12 metal ions reveals common preferential anchoring sites, the most populated one being His68; at higher metal ion concentration a second and a third site, close to the N-terminus of the protein, become populated and promote a polymorphic transition from orthorhombic to cubic form; Glu16 and Glu18, involved in the latter metal binding, undergo a remarkable displacement from their position in native ubiquitin; the aggregate stereochemistry appears to be driven by the clustering of deshielded backbone hydrogen-bond patches, and metal ions foster this process. Structural probing of Zn(ii), Cd(ii) and Hg(ii) binding to human ubiquitin.,Falini G, Fermani S, Tosi G, Arnesano F, Natile G Chem Commun (Camb). 2008 Dec 7;(45):5960-2. Epub 2008 Oct 9. PMID:19030552 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ubiquitin

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