1I9B: Acetylcholine binding protein

X-ray structure of acetylcholine binding protein (ACHBP). Determined by X-ray diffraction at 2.7 Å resolution. Released 16 May 2001.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Lymnaea stagnalis
Chains
5
Atoms
8,299
Mol. weight
124.95 kDa
Ligands
CA
Released
16 May 2001

Explore 1I9B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1I9B contains 20 α-helices and 75 β-strands across 5 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.

Chains A, B, C, D and E: 4 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix3-1311
β-strand2211
β-strand2511
α-helix261
β-strand27-42162
β-strand47-59132
α-helix61-633
β-strand73-7752
α-helix78-803
β-strand86-8833
β-strand9112
β-strand96-9722
β-strand102-10652
β-strand110-11342
β-strand116-12272
β-strand134-14293
β-strand150-15342
β-strand171-185153
β-strand188-203163

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Acetylcholine binding proteinA, B, C, D, Eprotein217Lymnaea stagnalisP58154 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E), FASTA
>1I9B_1 ACETYLCHOLINE BINDING PROTEIN (chains A, B, C, D, E)
EAEAYVEFDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFW
QQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLY
MPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEI
LDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa8

Water and common crystallization additives (EPE) are not listed.

Primary citation

Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Brejc, K., van Dijk, W.J., Klaassen, R.V. et al. Nature (2001) 411:269-276. DOI 10.1038/35077011 · PubMed

Other PDB entries of the same protein (UniProt P58154 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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1I9B is part of these collections:

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