8P11: Acetylcholine-binding protein

X-ray structure of acetylcholine-binding protein (AChBP) in complex with FL003044. Determined by X-ray diffraction at 1.9 Å resolution. Released 8 May 2024.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Lymnaea stagnalis
Chains
10
Atoms
16,962
Mol. weight
271.9 kDa
Ligands
WD5
Released
8 May 2024

Explore 8P11 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8P11 contains 42 α-helices and 150 β-strands across 10 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, E, F, H, I and J: 4 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix22-3211
β-strand4111
β-strand4411
α-helix451
β-strand46-61162
β-strand66-78132
α-helix80-823
β-strand92-9652
α-helix97-993
β-strand105-10733
β-strand11012
β-strand115-11622
β-strand121-12552
β-strand129-13242
β-strand135-14172
β-strand153-16193
β-strand169-17242
β-strand190-203143
β-strand210-222133
Chain G: 6 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix22-3211
β-strand41119
β-strand44119
α-helix451
β-strand46-611620
β-strand66-781320
α-helix80-823
β-strand92-96520
α-helix97-993
β-strand105-107321
β-strand110120
β-strand115-116220
β-strand121-125520
β-strand129-132420
β-strand135-141720
β-strand153-161921
β-strand169-172420
α-helix173-1753
β-strand190-2031421
β-strand210-2221321
α-helix223-2242

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Acetylcholine-binding proteinA, B, C, D, E, F, G, H, I, Jprotein237Lymnaea stagnalisP58154 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J), FASTA
>8P11_1 Acetylcholine-binding protein (chains A, B, C, D, E, F, G, H, I, J)
MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEV
NEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQ
LARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDD
SEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEILGSHHHHHH

Ligands and cofactors

IDNameFormulaCopies
WD54-(4-chlorophenyl)piperidin-4-olC11 H14 Cl N O4

Water and common crystallization additives (GOL, CL) are not listed.

Primary citation

Detection and characterisation of ligand-induced conformational changes in acetylcholine binding proteins using biosensors and X-ray crystallography. FitzGerald, E.A., Cederfelt, D., Kovryzhenko, D. et al. RSC Chem Biol (2025) 6:1625-1639. DOI 10.1039/d5cb00041f · 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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