NMR Structure of alpha-Bungarotoxin. Determined by solution NMR. Released 16 May 2001.
Explore 1IKC in 3D Show helices and sheets RCSB PDB PDBe
1IKC contains 0 α-helices and 6 β-strands across 1 chain. 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 | 23 | 1 | 1 |
| β-strand | 26 | 1 | 2 |
| β-strand | 27-28 | 2 | 3 |
| β-strand | 39-40 | 2 | 3 |
| β-strand | 57 | 1 | 2 |
| β-strand | 60 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| long neurotoxin 1 | A | protein | 74 | Bungarus multicinctus | P60615 (AlphaFold model) |
>1IKC_1 long neurotoxin 1 (chains A) IVCHTTATSPISAVTCPPGENLCYRKMWCDAFCSSRGKVVELGCAATCPSKKPYEEVTCC STDKCNPHPKQRPG
NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic acetylcholine receptor. Scarselli, M., Spiga, O., Ciutti, A. et al. Biochemistry (2002) 41:1457-1463. DOI 10.1021/bi011012f · 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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