3E6Z
1.0 A Structure of CusF-W44A-Cu(II) residues 10-88 from Escherichia coli
Summary for 3E6Z
Entry DOI | 10.2210/pdb3e6z/pdb |
Related | 1ZEQ 2qcp |
Descriptor | Cation efflux system protein cusF, COPPER (II) ION, ACETATE ION, ... (4 entities in total) |
Functional Keywords | copper-binding, beta-barrel, ob-fold, metalloprotein, metal resistance, copper chaperone, metal-binding, periplasm, metal binding protein |
Biological source | Escherichia coli |
Cellular location | Periplasm: P77214 |
Total number of polymer chains | 1 |
Total formula weight | 8898.73 |
Authors | Loftin, I.R. (deposition date: 2008-08-17, release date: 2009-07-07, Last modification date: 2023-08-30) |
Primary citation | Loftin, I.R.,Blackburn, N.J.,McEvoy, M.M. Tryptophan Cu(I)-pi interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF J.Biol.Inorg.Chem., 14:905-912, 2009 Cited by PubMed: 19381697DOI: 10.1007/s00775-009-0503-y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1 Å) |
Structure validation
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