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.
Explore 8P11 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 22-32 | 11 | |
| β-strand | 41 | 1 | 1 |
| β-strand | 44 | 1 | 1 |
| α-helix | 45 | 1 | |
| β-strand | 46-61 | 16 | 2 |
| β-strand | 66-78 | 13 | 2 |
| α-helix | 80-82 | 3 | |
| β-strand | 92-96 | 5 | 2 |
| α-helix | 97-99 | 3 | |
| β-strand | 105-107 | 3 | 3 |
| β-strand | 110 | 1 | 2 |
| β-strand | 115-116 | 2 | 2 |
| β-strand | 121-125 | 5 | 2 |
| β-strand | 129-132 | 4 | 2 |
| β-strand | 135-141 | 7 | 2 |
| β-strand | 153-161 | 9 | 3 |
| β-strand | 169-172 | 4 | 2 |
| β-strand | 190-203 | 14 | 3 |
| β-strand | 210-222 | 13 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 22-32 | 11 | |
| β-strand | 41 | 1 | 19 |
| β-strand | 44 | 1 | 19 |
| α-helix | 45 | 1 | |
| β-strand | 46-61 | 16 | 20 |
| β-strand | 66-78 | 13 | 20 |
| α-helix | 80-82 | 3 | |
| β-strand | 92-96 | 5 | 20 |
| α-helix | 97-99 | 3 | |
| β-strand | 105-107 | 3 | 21 |
| β-strand | 110 | 1 | 20 |
| β-strand | 115-116 | 2 | 20 |
| β-strand | 121-125 | 5 | 20 |
| β-strand | 129-132 | 4 | 20 |
| β-strand | 135-141 | 7 | 20 |
| β-strand | 153-161 | 9 | 21 |
| β-strand | 169-172 | 4 | 20 |
| α-helix | 173-175 | 3 | |
| β-strand | 190-203 | 14 | 21 |
| β-strand | 210-222 | 13 | 21 |
| α-helix | 223-224 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Acetylcholine-binding protein | A, B, C, D, E, F, G, H, I, J | protein | 237 | Lymnaea stagnalis | P58154 (AlphaFold model) |
>8P11_1 Acetylcholine-binding protein (chains A, B, C, D, E, F, G, H, I, J) MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEV NEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQ LARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDD SEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEILGSHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| WD5 | 4-(4-chlorophenyl)piperidin-4-ol | C11 H14 Cl N O | 4 |
Water and common crystallization additives (GOL, CL) are not listed.
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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