Structure of the human M1 muscarinic acetylcholine receptor bound to antagonist Tiotropium. Determined by X-ray diffraction at 2.7 Å resolution. Released 9 Mar 2016.
Explore 5CXV in 3D Show helices and sheets RCSB PDB PDBe
5CXV contains 25 α-helices and 6 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 |
|---|---|---|---|
| α-helix | 22-52 | 31 | |
| α-helix | 54-56 | 3 | |
| α-helix | 59-73 | 15 | |
| α-helix | 74-78 | 5 | |
| α-helix | 79-88 | 10 | |
| α-helix | 95-128 | 34 | |
| α-helix | 134-136 | 3 | |
| α-helix | 139-168 | 30 | |
| α-helix | 174 | 1 | |
| α-helix | 186-193 | 8 | |
| α-helix | 194-198 | 5 | |
| α-helix | 199-212 | 14 | |
| α-helix | 215-1010 | 14 | |
| β-strand | 1013-1014 | 2 | 1 |
| β-strand | 1015 | 1 | 2 |
| β-strand | 1016-1018 | 3 | 1 |
| β-strand | 1024-1027 | 4 | 1 |
| β-strand | 1030-1033 | 4 | 1 |
| α-helix | 1038-1049 | 12 | |
| β-strand | 1056 | 1 | 2 |
| α-helix | 1059-1079 | 21 | |
| α-helix | 1083-1089 | 7 | |
| α-helix | 1092-1111 | 20 | |
| α-helix | 1114-1121 | 8 | |
| α-helix | 1125-1132 | 8 | |
| α-helix | 1136-1140 | 5 | |
| α-helix | 1142-1154 | 13 | |
| α-helix | 358-390 | 33 | |
| α-helix | 397-406 | 10 | |
| α-helix | 409-421 | 13 | |
| α-helix | 425-433 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Muscarinic acetylcholine receptor M1,Endolysin,Muscarinic acetylcholine receptor M1 | A | protein | 515 | Homo sapiens, Enterobacteria phage T4 | P00720, P11229 (AlphaFold model) |
| FLAG peptide | C | protein | 7 | Enterobacteria phage T4 |
>5CXV_1 Muscarinic acetylcholine receptor M1,Endolysin,Muscarinic acetylcholine receptor M1 (chains A) MKTIIALSYIFCLVFADYKDDDDAAAQTSAPPAVSPQITVLAPGKGPWQVAFIGITTGLL SLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGT LACDLWLALDYVASQASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFV LWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRET ENRNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVI TKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSL RMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYFSLVKEKKAARTLSAIL LAFILTWTPYNIMVLVSTFCKDCVPETLWELGYWLCYVNSTINPMCYALCNKAFRDTFRL LLLCRWDKRRWRKIPKRPGSVHRTPSRQCHHHHHH
>5CXV_2 FLAG peptide (chains C) DYKDDDD
| ID | Name | Formula | Copies |
|---|---|---|---|
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 1 |
| 0HK | (1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-a… | C19 H22 N O4 S2 | 1 |
Water and common crystallization additives (GOL, PGE, EDO) are not listed.
Crystal structures of the M1 and M4 muscarinic acetylcholine receptors. Thal, D.M., Sun, B., Feng, D. et al. Nature (2016) 531:335-340. DOI 10.1038/nature17188 · PubMed
Other PDB entries of the same protein (UniProt P00720), best resolution first:
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