X-ray structure of acetylcholine binding protein (ACHBP). Determined by X-ray diffraction at 2.7 Å resolution. Released 16 May 2001.
Explore 1I9B in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-13 | 11 | |
| β-strand | 22 | 1 | 1 |
| β-strand | 25 | 1 | 1 |
| α-helix | 26 | 1 | |
| β-strand | 27-42 | 16 | 2 |
| β-strand | 47-59 | 13 | 2 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 2 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 3 |
| β-strand | 91 | 1 | 2 |
| β-strand | 96-97 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 110-113 | 4 | 2 |
| β-strand | 116-122 | 7 | 2 |
| β-strand | 134-142 | 9 | 3 |
| β-strand | 150-153 | 4 | 2 |
| β-strand | 171-185 | 15 | 3 |
| β-strand | 188-203 | 16 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Acetylcholine binding protein | A, B, C, D, E | protein | 217 | Lymnaea stagnalis | P58154 (AlphaFold model) |
>1I9B_1 ACETYLCHOLINE BINDING PROTEIN (chains A, B, C, D, E) EAEAYVEFDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFW QQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLY MPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEI LDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 8 |
Water and common crystallization additives (EPE) are not listed.
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:
1I9B is part of these collections:
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