The crystal structure of alpha-bungarotoxin at 2.5 Å resolution. Relation to solution structure and binding to acetylcholine receptor. Determined by X-ray diffraction at 2.5 Å resolution. Released 7 May 1986.
Explore 2ABX in 3D Show helices and sheets RCSB PDB PDBe
2ABX contains 0 α-helices and 7 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 | 25-26 | 2 | 1 |
| β-strand | 41-42 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 2 |
| β-strand | 13-14 | 2 | 2 |
| β-strand | 24-26 | 3 | 3 |
| β-strand | 41-42 | 2 | 3 |
| β-strand | 57-59 | 3 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-bungarotoxin | A, B | protein | 74 | Bungarus multicinctus | P60615 (AlphaFold model) |
>2ABX_1 ALPHA-BUNGAROTOXIN (chains A, B) IVCHTTATIPSSAVTCPPGENLCYRKMWCDAFCSSRGKVVELGCAATCPSKKPYEEVTCC STDKCNHPPKRQPG
The crystal structure of alpha-bungarotoxin at 2.5 A resolution: relation to solution structure and binding to acetylcholine receptor. Love, R.A., Stroud, R.M. Protein Eng (1986) 1:37-46. DOI 10.1093/protein/1.1.37 · 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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