3C1H
Substrate binding, deprotonation and selectivity at the periplasmic entrance of the E. coli ammonia channel AmtB
Summary for 3C1H
Entry DOI | 10.2210/pdb3c1h/pdb |
Related | 1U7G 1XQF 2B2F 3B9W 3C1G 3C1I 3C1J |
Descriptor | Ammonia channel, ACETATE ION, LAURYL DIMETHYLAMINE-N-OXIDE, ... (5 entities in total) |
Functional Keywords | transport protein, membrane protein, ammonia transport, phe-gate mutant, amtb, inner membrane, transmembrane |
Biological source | Escherichia coli |
Cellular location | Cell inner membrane; Multi-pass membrane protein: P69681 |
Total number of polymer chains | 1 |
Total formula weight | 44733.15 |
Authors | Lupo, D.,Winkler, F.K. (deposition date: 2008-01-23, release date: 2008-03-18, Last modification date: 2023-11-01) |
Primary citation | Javelle, A.,Lupo, D.,Ripoche, P.,Fulford, T.,Merrick, M.,Winkler, F.K. Substrate binding, deprotonation, and selectivity at the periplasmic entrance of the Escherichia coli ammonia channel AmtB. Proc.Natl.Acad.Sci.Usa, 105:5040-5045, 2008 Cited by PubMed: 18362341DOI: 10.1073/pnas.0711742105 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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