1NAQ
Crystal structure of CUTA1 from E.coli at 1.7 A resolution
Summary for 1NAQ
Entry DOI | 10.2210/pdb1naq/pdb |
Related | 1KR4 |
Descriptor | Periplasmic divalent cation tolerance protein cutA, MERCURY (II) ION, MERCURIBENZOIC ACID, ... (4 entities in total) |
Functional Keywords | cuta, copper resistance, structural proteomics in europe, spine, structural genomics, electron transport |
Biological source | Escherichia coli |
Cellular location | Cytoplasm : P69488 |
Total number of polymer chains | 6 |
Total formula weight | 78873.90 |
Authors | Calderone, V.,Mangani, S.,Benvenuti, M.,Viezzoli, M.S.,Banci, L.,Bertini, I.,Structural Proteomics in Europe (SPINE) (deposition date: 2002-11-28, release date: 2003-11-25, Last modification date: 2024-02-14) |
Primary citation | Arnesano, F.,Banci, L.,Benvenuti, M.,Bertini, I.,Calderone, V.,Mangani, S.,Viezzoli, M.S. The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transduction. J.Biol.Chem., 278:45999-46006, 2003 Cited by PubMed: 12949080DOI: 10.1074/jbc.M304398200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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