1LJZ: AChR-peptide

NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin. Determined by solution NMR. Released 17 Jul 2002.

Method
Solution NMR
Organism
Bungarus multicinctus
Chains
2
Atoms
772
Mol. weight
11.14 kDa
Released
17 Jul 2002

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

Secondary structure: helices and β-sheets

1LJZ contains 1 α-helix and 11 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, 8 β-strands

ElementResiduesLengthSheet
β-strand4-521
β-strand12-1321
β-strand22-2762
β-strand29-3133
β-strand37-3823
β-strand4014
β-strand41-4552
β-strand56-6052
Chain B: 1 helix, 3 β-strands
ElementResiduesLengthSheet
β-strand186-18835
β-strand18914
α-helix1971
β-strand198-20035

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
alpha-BungarotoxinAprotein74Bungarus multicinctusP60615 (AlphaFold model)
Acetylcholine receptor proteinBprotein25P02711 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1LJZ_1 alpha-Bungarotoxin (chains A)
IVCHTTATSPISAVTCPPGENLCYRKMWCDAFCSSRGKVVELGCAATCPSKKPYEEVTCC
STDKCNPHPKQRPG
Sequence of entity 2 (B), FASTA
>1LJZ_2 Acetylcholine receptor protein (chains B)
EERGWKHWVYYTCCPDTPYLDITEE

Primary citation

The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR. Samson, A., Scherf, T., Eisenstein, M. et al. Neuron (2002) 35:319-332. DOI 10.1016/S0896-6273(02)00773-0 · 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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