3C1H

Substrate binding, deprotonation and selectivity at the periplasmic entrance of the E. coli ammonia channel AmtB

Summary for 3C1H

Related1XQF 1U7G 2B2F 3B9W 3C1G 3C1I 3C1J
DescriptorAmmonia channel, ACETATE ION, LAURYL DIMETHYLAMINE-N-OXIDE, ... (5 entities in total)
Functional Keywordstransport protein, membrane protein, ammonia transport, phe-gate mutant, amtb, inner membrane, transmembrane
Biological sourceEscherichia coli
Cellular locationCell inner membrane; Multi-pass membrane protein P69681
Total number of polymer chains1
Total molecular weight44733.15
Authors
Lupo, D.,Winkler, F.K. (deposition date: 2008-01-23, release date: 2008-03-18, Last modification date: 2017-10-25)
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
PubMed: 18362341 (PDB entries with the same primary citation)
DOI: 10.1073/pnas.0711742105
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.2 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliers 0.267120 3.4%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
170383
PDB entries from 2020-10-28