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; PubMed: 19381697; DOI: 10.1007/s00775-009-0503-y

Experimental method

X-RAY DIFFRACTION (1 Å)