Solution NMR structure of the complex of alpha-bungarotoxin with a library derived peptide, 20 structures. Determined by solution NMR. Released 27 Jan 1999.
Explore 1BXP in 3D Show helices and sheets RCSB PDB PDBe
1BXP contains 0 α-helices and 5 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 | 2-4 | 3 | 1 |
| β-strand | 13-15 | 3 | 1 |
| β-strand | 22-26 | 5 | 2 |
| β-strand | 41-45 | 5 | 2 |
| β-strand | 60 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-bungarotoxin | A | protein | 74 | Bungarus multicinctus | P60615 (AlphaFold model) |
| Peptide met-arg-tyr-tyr-glu-ser-ser-leu-lys-ser-tyr-pro-asp | B | protein | 13 |
>1BXP_1 ALPHA-BUNGAROTOXIN (chains A) IVCHTTATSPISAVTCPPGENLCYRKMWCDAFCSSRGKVVELGCAATCPSKKPYEEVTCC STDKCNPHPKQRPG
>1BXP_2 PEPTIDE MET-ARG-TYR-TYR-GLU-SER-SER-LEU-LYS-SER-TYR-PRO-ASP (chains B) MRYYESSLKSYPD
Three-dimensional solution structure of the complex of alpha-bungarotoxin with a library-derived peptide. Scherf, T., Balass, M., Fuchs, S. et al. Proc Natl Acad Sci U S A (1997) 94:6059-6064. DOI 10.1073/pnas.94.12.6059 · 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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