alpha-bungarotoxin complexed with high affinity peptide. Determined by X-ray diffraction at 1.8 Å resolution. Released 10 Nov 2001.
Explore 1HC9 in 3D Show helices and sheets RCSB PDB PDBe
1HC9 contains 7 α-helices and 13 β-strands across 4 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 | 2-5 | 4 | 1 |
| β-strand | 12-15 | 4 | 1 |
| α-helix | 16-17 | 2 | |
| β-strand | 22-28 | 7 | 2 |
| α-helix | 33-36 | 4 | |
| β-strand | 39-45 | 7 | 2 |
| α-helix | 48-50 | 3 | |
| β-strand | 56-60 | 5 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-5 | 4 | 3 |
| β-strand | 12-15 | 4 | 3 |
| α-helix | 16-17 | 2 | |
| β-strand | 22-28 | 7 | 4 |
| α-helix | 33-36 | 4 | |
| β-strand | 39-45 | 7 | 4 |
| α-helix | 48-52 | 5 | |
| β-strand | 56-60 | 5 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 2 |
| β-strand | 7-11 | 5 | 2 |
| α-helix | 12 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-bungarotoxin isoform V31 | A | protein | 74 | BUNGARUS MULTICINCTUS | P60616 (AlphaFold model) |
| Alpha-bungarotoxin isoform A31 | B | protein | 74 | BUNGARUS MULTICINCTUS | P60615 (AlphaFold model) |
| Peptide inhibitor | C, D | protein | 13 | SYNTHETIC CONSTRUCT |
>1HC9_1 ALPHA-BUNGAROTOXIN ISOFORM V31 (chains A) IVCHTTATSPISAVTCPPGENLCYRKMWCDVFCSSRGKVVELGCAATCPSKKPYEEVTCC STDKCNPHPKQRPG
>1HC9_2 ALPHA-BUNGAROTOXIN ISOFORM A31 (chains B) IVCHTTATSPISAVTCPPGENLCYRKMWCDAFCSSRGKVVELGCAATCPSKKPYEEVTCC STDKCNPHPKQRPG
>1HC9_3 PEPTIDE INHIBITOR (chains C, D) WRYYESSLLPYPD
The Binding Site of Acetylcholine Receptor as Visualized in the X-Ray Structure of a Complex between Alpha-Bungarotoxin and a Mimotope Peptide. Harel, M., Kasher, R., Nicolas, A. et al. Neuron (2001) 32:265. DOI 10.1016/S0896-6273(01)00461-5 · PubMed
Other PDB entries of the same protein (UniProt P60616 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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