1JWW
NMR characterization of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis
Summary for 1JWW
| Entry DOI | 10.2210/pdb1jww/pdb |
| Descriptor | Potential copper-transporting ATPase (1 entity in total) |
| Functional Keywords | beta-alpha-beta-beta-alpha-beta, hydrolase |
| Biological source | Bacillus subtilis |
| Cellular location | Cell membrane; Multi-pass membrane protein: O32220 |
| Total number of polymer chains | 1 |
| Total formula weight | 8799.97 |
| Authors | Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,D'Onofrio, M.,Gonnelli, L.,Marhuenda-Egea, F.,Ruiz-Duenas, F.J. (deposition date: 2001-09-05, release date: 2002-04-10, Last modification date: 2022-02-23) |
| Primary citation | Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,D'Onofrio, M.,Gonnelli, L.,Marhuenda-Egea, F.C.,Ruiz-Duenas, F.J. Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states. J.Mol.Biol., 317:415-429, 2002 Cited by PubMed: 11922674DOI: 10.1006/jmbi.2002.5430 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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