1BXP: Alpha-bungarotoxin

Solution NMR structure of the complex of alpha-bungarotoxin with a library derived peptide, 20 structures. Determined by solution NMR. Released 27 Jan 1999.

Method
Solution NMR
Organism
Bungarus multicinctus
Chains
2
Atoms
666
Mol. weight
9.65 kDa
Released
27 Jan 1999

Explore 1BXP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 0 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand2-431
β-strand13-1531
β-strand22-2652
β-strand41-4552
β-strand6012

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-bungarotoxinAprotein74Bungarus multicinctusP60615 (AlphaFold model)
Peptide met-arg-tyr-tyr-glu-ser-ser-leu-lys-ser-tyr-pro-aspBprotein13
Sequence of entity 1 (A), FASTA
>1BXP_1 ALPHA-BUNGAROTOXIN (chains A)
IVCHTTATSPISAVTCPPGENLCYRKMWCDAFCSSRGKVVELGCAATCPSKKPYEEVTCC
STDKCNPHPKQRPG
Sequence of entity 2 (B), FASTA
>1BXP_2 PEPTIDE MET-ARG-TYR-TYR-GLU-SER-SER-LEU-LYS-SER-TYR-PRO-ASP (chains B)
MRYYESSLKSYPD

Primary citation

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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