9E3F: Acetylcholine receptor subunit alpha
Torpedo muscle-type nicotinic acetylcholine receptor - Unliganded State. Determined by electron microscopy at 3.2 Å resolution. Released 8 Oct 2025.
- Method
- Electron microscopy
- Resolution
- 3.2 Å
- Organism
- Tetronarce californica
- Chains
- 5
- Atoms
- 17,181
- Mol. weight
- 281.17 kDa
- Ligands
- POV
- Released
- 8 Oct 2025
Explore 9E3F in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9E3F contains 68 α-helices and 80 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.
Chain A: 13 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-11 | 10 | |
| β-strand | 29-44 | 16 | 1 |
| β-strand | 49-61 | 13 | 1 |
| α-helix | 69-71 | 3 | |
| β-strand | 78-80 | 3 | 1 |
| β-strand | 90-92 | 3 | 2 |
| β-strand | 95 | 1 | 1 |
| β-strand | 108-110 | 3 | 1 |
| β-strand | 115-118 | 4 | 1 |
| β-strand | 121-127 | 7 | 1 |
| β-strand | 139-148 | 10 | 2 |
| β-strand | 156-160 | 5 | 1 |
| β-strand | 166 | 1 | 1 |
| β-strand | 176-190 | 15 | 2 |
| β-strand | 193-209 | 17 | 2 |
| α-helix | 210 | 1 | |
| α-helix | 212-214 | 3 | |
| α-helix | 215-219 | 5 | |
| α-helix | 220-229 | 10 | |
| α-helix | 230-234 | 5 | |
| α-helix | 242-263 | 22 | |
| α-helix | 273-299 | 27 | |
| α-helix | 307-309 | 3 | |
| α-helix | 310-318 | 9 | |
| α-helix | 320-323 | 4 | |
| α-helix | 370-433 | 64 | |
Chain B: 15 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-11 | 9 | |
| β-strand | 29-44 | 16 | 3 |
| β-strand | 49-61 | 13 | 3 |
| α-helix | 69-71 | 3 | |
| β-strand | 77-80 | 4 | 3 |
| β-strand | 90-92 | 3 | 4 |
| β-strand | 95 | 1 | 3 |
| α-helix | 106-107 | 2 | |
| β-strand | 108-111 | 4 | 3 |
| β-strand | 115-118 | 4 | 3 |
| β-strand | 121-127 | 7 | 3 |
| β-strand | 139-148 | 10 | 4 |
| β-strand | 156-160 | 5 | 3 |
| β-strand | 162 | 1 | 5 |
| β-strand | 169 | 1 | 5 |
| β-strand | 172 | 1 | 6 |
| β-strand | 174-175 | 2 | 3 |
| α-helix | 181-183 | 3 | |
| β-strand | 186-190 | 5 | 4 |
| β-strand | 192 | 1 | 6 |
| β-strand | 193-195 | 3 | 4 |
| β-strand | 207-215 | 9 | 4 |
| α-helix | 218-220 | 3 | |
| α-helix | 221-225 | 5 | |
| α-helix | 226-238 | 13 | |
| α-helix | 243-245 | 3 | |
| α-helix | 248-269 | 22 | |
| α-helix | 279-305 | 27 | |
| α-helix | 316-319 | 4 | |
| α-helix | 320-325 | 6 | |
| α-helix | 326-329 | 4 | |
| α-helix | 402-459 | 58 | |
| α-helix | 462-464 | 3 | |
Chain C: 15 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-8 | 6 | |
| α-helix | 9-14 | 6 | |
| β-strand | 31-46 | 16 | 7 |
| β-strand | 51-63 | 13 | 7 |
| α-helix | 65-67 | 3 | |
| β-strand | 80-82 | 3 | 7 |
| α-helix | 84-86 | 3 | |
| β-strand | 93-94 | 2 | 8 |
| α-helix | 108-109 | 2 | |
| β-strand | 110-112 | 3 | 7 |
| β-strand | 117-120 | 4 | 7 |
| β-strand | 123-129 | 7 | 7 |
| β-strand | 141-149 | 9 | 8 |
| β-strand | 158-162 | 5 | 7 |
| α-helix | 163 | 1 | |
| β-strand | 164-167 | 4 | 9 |
| β-strand | 170-173 | 4 | 9 |
| β-strand | 176 | 1 | 10 |
| β-strand | 178 | 1 | 7 |
| β-strand | 190-192 | 3 | 8 |
| β-strand | 196 | 1 | 10 |
| β-strand | 197-201 | 5 | 8 |
| β-strand | 213-223 | 11 | 8 |
| α-helix | 224 | 1 | |
| α-helix | 226-228 | 3 | |
| α-helix | 229-233 | 5 | |
| α-helix | 234-244 | 11 | |
| α-helix | 245-247 | 3 | |
| α-helix | 256-276 | 21 | |
| α-helix | 287-313 | 27 | |
| α-helix | 324-338 | 15 | |
| α-helix | 419-477 | 59 | |
Chain D: 14 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-12 | 11 | |
| β-strand | 29-44 | 16 | 11 |
| β-strand | 49-61 | 13 | 11 |
| α-helix | 69-72 | 4 | |
| β-strand | 77-81 | 5 | 11 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-92 | 3 | 12 |
| β-strand | 95 | 1 | 11 |
| β-strand | 107-111 | 5 | 11 |
| β-strand | 115-118 | 4 | 11 |
| β-strand | 121-126 | 6 | 11 |
| β-strand | 139-148 | 10 | 12 |
| β-strand | 156-160 | 5 | 11 |
| β-strand | 166 | 1 | 11 |
| α-helix | 170-172 | 3 | |
| β-strand | 176-188 | 13 | 12 |
| β-strand | 198-209 | 12 | 12 |
| α-helix | 212-214 | 3 | |
| α-helix | 215-219 | 5 | |
| α-helix | 220-231 | 12 | |
| α-helix | 232-234 | 3 | |
| α-helix | 242-263 | 22 | |
| α-helix | 273-299 | 27 | |
| α-helix | 310-313 | 4 | |
| α-helix | 314-319 | 6 | |
| α-helix | 320-323 | 4 | |
| β-strand | 329 | 1 | 13 |
| α-helix | 377-434 | 58 | |
Chain E: 11 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-11 | 9 | |
| β-strand | 29-44 | 16 | 14 |
| β-strand | 49-61 | 13 | 14 |
| β-strand | 77-80 | 4 | 14 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-92 | 3 | 15 |
| β-strand | 95 | 1 | 14 |
| β-strand | 108-111 | 4 | 14 |
| β-strand | 115-118 | 4 | 14 |
| β-strand | 121-127 | 7 | 14 |
| β-strand | 139-148 | 10 | 15 |
| β-strand | 156-160 | 5 | 14 |
| β-strand | 162 | 1 | 16 |
| β-strand | 167 | 1 | 16 |
| β-strand | 170 | 1 | 17 |
| β-strand | 184-188 | 5 | 15 |
| β-strand | 190 | 1 | 17 |
| β-strand | 191-195 | 5 | 15 |
| β-strand | 207-217 | 11 | 15 |
| α-helix | 218 | 1 | |
| α-helix | 220-222 | 3 | |
| α-helix | 223-227 | 5 | |
| α-helix | 228-236 | 9 | |
| α-helix | 237-242 | 6 | |
| α-helix | 251-269 | 19 | |
| α-helix | 282-308 | 27 | |
| β-strand | 315 | 1 | 13 |
| α-helix | 319-327 | 9 | |
| α-helix | 418-472 | 55 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Acetylcholine receptor subunit alpha | A, D | protein | 437 | Tetronarce californica | P02710 (AlphaFold model) |
| Acetylcholine receptor subunit beta | B | protein | 469 | Tetronarce californica | P02712 (AlphaFold model) |
| Acetylcholine receptor subunit delta | C | protein | 501 | Tetronarce californica | P02718 (AlphaFold model) |
| Acetylcholine receptor subunit gamma | E | protein | 488 | Tetronarce californica | P02714 (AlphaFold model) |
Sequence of entity 1 (A, D), FASTA
>9E3F_1 Acetylcholine receptor subunit alpha (chains A, D)
SEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQLIQLISVDEVNQIVETNVRLRQQW
IDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNADGDFAIVHMTKLLLDYTGKIMWTP
PAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKVSISPESDRPDLSTFMESGEWVMKD
YRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVVNVIIPCLLFSFLTGLVFYLPTDSG
EKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIITVVVINTHH
RSPSTHTMPQWVRKIFIDTIPNVMFFSTMKRASKEKQENKIFADDIDISDISGKQVTGEV
IFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICII
GTVSVFAGRLIELSQEG
Sequence of entity 2 (B), FASTA
>9E3F_2 Acetylcholine receptor subunit beta (chains B)
SVMEDTLLSVLFETYNPKVRPAQTVGDKVTVRVGLTLTNLLILNEKIEEMTTNVFLNLAW
TDYRLQWDPAAYEGIKDLRIPSSDVWQPDIVLMNNNDGSFEITLHVNVLVQHTGAVSWQP
SAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEVTLQHALDAKGEREVKEIVINKDAF
TENGQWSIEHKPSRKNWRSDDPSYEDVTFYLIIQRKPLFYIVYTIIPCILISILAILVFY
LPPDAGEKMSLSISALLAVTVFLLLLADKVPETSLSVPIIIRYLMFIMILVAFSVILSVV
VLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPVTTPSPDSKPTIISRANDEYFIRKP
AGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVTLPQDLKEAVEAIKYIAEQLESASE
FDDLKKDWQYVAMVADRLFLYVFFVICSIGTFSIFLDASHNVPPDNPFA
Sequence of entity 3 (C), FASTA
>9E3F_3 Acetylcholine receptor subunit delta (chains C)
VNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTSNVWMDH
AWYDHRLTWNASEYSDISILRLPPELVWIPDIVLQNNNDGQYHVAYFCNVLVRPNGYVTW
LPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYDANEITMDLMTDTIDGKDYPIEWIIID
PEAFTENGEWEIIHKPAKKNIYPDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLIS
FLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVT
GVIVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRADESEQPDWQNDLKLRRS
SSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGNNNENIAASDQLHDEIK
SGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNH
PPAKPFEGDPFDYSSDHPRCA
Sequence of entity 4 (E), FASTA
>9E3F_4 Acetylcholine receptor subunit gamma (chains E)
NEEGRLIEKLLGDYDKRIIPAKTLDHIIDVTLKLTLTNLISLNEKEEALTTNVWIEIQWN
DYRLSWNTSEYEGIDLVRIPSELLWLPDVVLENNVDGQFEVAYYANVLVYNDGSMYWLPP
AIYRSTCPIAVTYFPFDWQNCSLVFRSQTYNAHEVNLQLSAEEGEAVEWIHIDPEDFTEN
GEWTIRHRPAKKNYNWQLTKDDTDFQEIIFFLIIQRKPLFYIINIIAPCVLISSLVVLVY
FLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSMLIVMNC
VIVLNVSLRTPNTHSLSEKIKHLFLGFLPKYLGMQLEPSEETPEKPQPRRRSSFGIMIKA
EEYILKKPRSELMFEEQKDRHGLKRVNKMTSDIDIGTTVDLYKDLANFAPEIKSCVEACN
FIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLLFSIGTLAIFLTGHFNQVPEFPFP
GDPRKYVP
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| POV | (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl… | C42 H82 N O8 P | 8 |
Primary citation
Asynchronous subunit transitions prime acetylcholine receptor activation. Thompson, M.J., Tessier, C.J.G., Ananchenko, A. et al. Science (2026) 391:eadw1264-eadw1264. DOI 10.1126/science.adw1264 · PubMed
Other PDB entries of the same protein (UniProt P02710 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8YQN 2.27 Å, Torpedo acetylcholine receptor in complex with Erabutoxin A
- 7QL5 2.5 Å, Torpedo muscle-type nicotinic acetylcholine receptor - nicotine-bound conformation
- 7SMM 2.5 Å, Cryo-EM structure of Torpedo acetylcholine receptor in apo form
- 7SMT 2.56 Å, Cryo-EM structure of Torpedo acetylcholine receptor in complex with d-tubocurarine and…
- 6UWZ 2.69 Å, Cryo-EM structure of Torpedo acetylcholine receptor in complex with alpha-bungarotoxin
- 8F6Z 2.7 Å, Cryo-EM structure of Torpedo nicotinic acetylcholine receptor in complex with…
- 7SMQ 2.74 Å, Cryo-EM structure of Torpedo acetylcholine receptor in apo form with added cholesterol
- 7SMR 2.77 Å, Cryo-EM structure of Torpedo acetylcholine receptor in complex with carbachol,…
- 8F6Y 2.79 Å, Cryo-EM structure of Torpedo nicotinic acetylcholine receptor in complex with etomidate,…
- 9E3E 2.8 Å, Torpedo muscle-type nicotinic acetylcholine receptor - Diliganded State
- 7QKO 2.9 Å, Torpedo muscle-type nicotinic acetylcholine receptor - Resting conformation
- 8ESK 2.9 Å, Cryo-EM structure of Torpedo nicotinic acetylcholine receptor in complex with…
Browse structure collections
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