NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin. Determined by solution NMR. Released 17 Jul 2002.
Explore 1L4W in 3D Show helices and sheets RCSB PDB PDBe
1L4W contains 0 α-helices and 8 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 1 |
| β-strand | 11-15 | 5 | 1 |
| β-strand | 22-31 | 10 | 2 |
| β-strand | 37-45 | 9 | 2 |
| β-strand | 56-60 | 5 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 186-188 | 3 | 3 |
| β-strand | 189-191 | 3 | 2 |
| β-strand | 198-200 | 3 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| alpha-Bungarotoxin | A | protein | 74 | Bungarus multicinctus | P60615 (AlphaFold model) |
| Acetylcholine receptor protein | B | protein | 25 | P02711 (AlphaFold model) |
>1L4W_1 alpha-Bungarotoxin (chains A) IVCHTTATSPISAVTCPPGENLCYRKMWCDAFCSSRGKVVELGCAATCPSKKPYEEVTCC STDKCNPHPKQRPG
>1L4W_2 Acetylcholine receptor protein (chains B) EERGWKHWVYYTCCPDTPYLDITEE
The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR. Samson, A., Scherf, T., Eisenstein, M. et al. Neuron (2002) 35:319-332. DOI 10.1016/S0896-6273(02)00773-0 · PubMed
Other PDB entries of the same protein (UniProt P60615 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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