Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. Determined by X-ray diffraction at 2.8 Å resolution. Released 31 Aug 1994.
Explore 1ACJ in 3D Show helices and sheets RCSB PDB PDBe
1ACJ contains 37 α-helices and 22 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 7-10 | 4 | 1 |
| β-strand | 13-16 | 4 | 1 |
| β-strand | 18-22 | 5 | 2 |
| β-strand | 25-34 | 10 | 2 |
| β-strand | 36-37 | 2 | 3 |
| α-helix | 41-43 | 3 | |
| α-helix | 47-48 | 2 | |
| β-strand | 49-50 | 2 | 3 |
| α-helix | 51-53 | 3 | |
| β-strand | 57-59 | 3 | 1 |
| α-helix | 65 | 1 | |
| β-strand | 66 | 1 | 4 |
| α-helix | 67-68 | 2 | |
| α-helix | 70-72 | 3 | |
| α-helix | 79-82 | 4 | |
| β-strand | 90 | 1 | 4 |
| β-strand | 96-101 | 6 | 2 |
| α-helix | 105-106 | 2 | |
| β-strand | 109-115 | 7 | 2 |
| α-helix | 128-130 | 3 | |
| α-helix | 133-139 | 7 | |
| β-strand | 142-145 | 4 | 2 |
| α-helix | 152-155 | 4 | |
| α-helix | 168-183 | 16 | |
| α-helix | 184-187 | 4 | |
| β-strand | 189-199 | 11 | 2 |
| α-helix | 201-211 | 11 | |
| α-helix | 213-216 | 4 | |
| β-strand | 221-225 | 5 | 2 |
| β-strand | 236-237 | 2 | 5 |
| α-helix | 238-251 | 14 | |
| α-helix | 259-268 | 10 | |
| α-helix | 271-278 | 8 | |
| α-helix | 279-281 | 3 | |
| β-strand | 295-296 | 2 | 5 |
| α-helix | 305-311 | 7 | |
| β-strand | 319-324 | 6 | 2 |
| β-strand | 326 | 1 | 6 |
| α-helix | 329-335 | 7 | |
| α-helix | 346-348 | 3 | |
| α-helix | 349-359 | 11 | |
| α-helix | 365-375 | 11 | |
| α-helix | 378-380 | 3 | |
| α-helix | 384-396 | 13 | |
| α-helix | 397-401 | 5 | |
| α-helix | 402-412 | 11 | |
| β-strand | 418-423 | 6 | 2 |
| α-helix | 434-436 | 3 | |
| β-strand | 439 | 1 | 6 |
| α-helix | 444-447 | 4 | |
| α-helix | 450-452 | 3 | |
| α-helix | 454-456 | 3 | |
| α-helix | 460-478 | 19 | |
| α-helix | 493-495 | 3 | |
| β-strand | 501-505 | 5 | 2 |
| β-strand | 512-514 | 3 | 2 |
| α-helix | 518-522 | 5 | |
| α-helix | 523-527 | 5 | |
| α-helix | 528-534 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Acetylcholinesterase | A | protein | 537 | Torpedo californica | P04058 (AlphaFold model) |
>1ACJ_1 ACETYLCHOLINESTERASE (chains A) DDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNA STYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGF YSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWV HDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAE GRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEF FPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSV PHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYL YFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTG NPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATET
| ID | Name | Formula | Copies |
|---|---|---|---|
| THA | Tacrine | C13 H14 N2 | 1 |
Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. Harel, M., Schalk, I., Ehret-Sabatier, L. et al. Proc Natl Acad Sci U S A (1993) 90:9031-9035. DOI 10.1073/pnas.90.19.9031 · PubMed
Other PDB entries of the same protein (UniProt P04058 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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