1LJZ

NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin

Summary for 1LJZ

Related1l4w
Descriptoralpha-Bungarotoxin, Acetylcholine receptor protein (2 entities in total)
Functional Keywordsbungarotoxin, acetylcholine receptor, beta-hairpin, intermolecular beta-sheet, receptor, toxin
Biological sourceBungarus multicinctus (many-banded krait)
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Cellular locationSecreted P60615
Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein P02711
Total number of polymer chains2
Total molecular weight11142.71
Authors
Samson, A.O.,Scherf, T.,Eisenstein, M.,Chill, J.H.,Anglister, J. (deposition date: 2002-04-23, release date: 2002-07-17, Last modification date: 2013-07-24)
Primary citation
Samson, A.,Scherf, T.,Eisenstein, M.,Chill, J.,Anglister, J.
The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR.
Neuron, 35:319-332, 2002
PubMed: 12160749 (PDB entries with the same primary citation)
DOI: 10.1016/S0896-6273(02)00773-0
MImport into Mendeley
Experimental method
SOLUTION NMR
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers919.9%30.2%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures
Download full validation reportDownload