Structure of acetylcholine receptor pore from electron images. Determined by electron microscopy at 4.0 Å resolution. Released 26 Jun 2003.
Explore 1OED in 3D Show helices and sheets RCSB PDB PDBe
1OED contains 24 α-helices and 0 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 | 213-238 | 26 | |
| α-helix | 240-242 | 3 | |
| α-helix | 243-270 | 28 | |
| α-helix | 276-301 | 26 | |
| α-helix | 405-436 | 32 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 219-244 | 26 | |
| α-helix | 246-248 | 3 | |
| α-helix | 249-276 | 28 | |
| α-helix | 284-306 | 23 | |
| α-helix | 433-461 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 227-252 | 26 | |
| α-helix | 257-284 | 28 | |
| α-helix | 290-315 | 26 | |
| α-helix | 453-483 | 31 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 222-227 | 6 | |
| α-helix | 229-245 | 17 | |
| α-helix | 251-279 | 29 | |
| α-helix | 286-310 | 25 | |
| α-helix | 446-477 | 32 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Acetylcholine receptor subunit alpha | A, D | protein | 227 | Torpedo marmorata | P02711 (AlphaFold model) |
| Acetylcholine receptor beta subunit | B | protein | 250 | Torpedo marmorata | P02712 (AlphaFold model) |
| Acetylcholine receptor delta subunit | C | protein | 260 | Torpedo marmorata | P02718 (AlphaFold model) |
| Acetylcholine receptor gamma subunit | E | protein | 260 | Torpedo marmorata | P02714 (AlphaFold model) |
>1OED_1 Acetylcholine receptor subunit alpha (chains A, D) PLYFVVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSA VPLIGKYMLFTMIFVISSIIITVVVINTHHRSPSTHTMPQWVRKIFIDTIPNVMFFSTMK RASKEKQENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDE ESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG
>1OED_2 Acetylcholine receptor beta subunit (chains B) PLFYIVYTIIPCILISILAILVFYLPPDAGEKMSLSISALLAVTVFLLLLADKVPETSLS VPIIIRYLMFIMILVAFSVILSVVVLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPV TTPSPDSKPTIISRANDEYFIRKPAGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVT LPQDLKEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYVFFVICSIGTFSIFL DASHNVPPDN
>1OED_3 Acetylcholine receptor delta subunit (chains C) PLFYVINFITPCVLISFLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLPETALA VPLIGKYLMFIMSLVTGVIVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRAD ESEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGN NNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPV MVLGTIFIFVMGNFNHPPAK
>1OED_4 Acetylcholine receptor gamma subunit (chains E) PLFYIINIIAPCVLISSLVVLVYFLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSL NVPLIGKYLIFVMFVSMLIVMNCVIVLNVSLRTPNTHSLSEKIKHLFLGFLPKYLGMQLE PSEETPEKPQPRRRSSFGIMIKAEEYILKKPRSELMFEEQKDRHGLKRVNKMTSDIDIGT TVDLYKDLANFAPEIKSCVEACNFIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLL FSIGTLAIFLTGHFNQVPEF
Structure and Gating Mechanism of the Acetylcholine Receptor Pore. Miyazawa, A., Fujiyoshi, Y., Unwin, N. Nature (2003) 423:949. DOI 10.1038/NATURE01748 · PubMed
Other PDB entries of the same protein (UniProt P02711 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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