2ABX: Alpha-bungarotoxin

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.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Bungarus multicinctus
Chains
2
Atoms
1,118
Mol. weight
16.01 kDa
Released
7 May 1986

Explore 2ABX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 0 helices, 2 β-strands

ElementResiduesLengthSheet
β-strand25-2621
β-strand41-4221
Chain B: 0 helices, 5 β-strands
ElementResiduesLengthSheet
β-strand4-522
β-strand13-1422
β-strand24-2633
β-strand41-4223
β-strand57-5933

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-bungarotoxinA, Bprotein74Bungarus multicinctusP60615 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2ABX_1 ALPHA-BUNGAROTOXIN (chains A, B)
IVCHTTATIPSSAVTCPPGENLCYRKMWCDAFCSSRGKVVELGCAATCPSKKPYEEVTCC
STDKCNHPPKRQPG

Primary citation

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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