Muscarinic acetylcholine receptor 1 - muscarinic toxin 7 complex. Determined by X-ray diffraction at 2.55 Å resolution. Released 8 Jul 2020.
Explore 6WJC in 3D Show helices and sheets RCSB PDB PDBe
6WJC contains 25 α-helices and 12 β-strands across 2 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 | 23-52 | 30 | |
| α-helix | 59-73 | 15 | |
| α-helix | 74-78 | 5 | |
| α-helix | 79-88 | 10 | |
| α-helix | 94-128 | 35 | |
| α-helix | 134-136 | 3 | |
| α-helix | 141-167 | 27 | |
| α-helix | 181-183 | 3 | |
| α-helix | 186-192 | 7 | |
| α-helix | 193-198 | 6 | |
| α-helix | 199-1010 | 30 | |
| 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 | 1038-1048 | 11 | |
| β-strand | 1056 | 1 | 2 |
| α-helix | 1059-1078 | 20 | |
| α-helix | 1083-1089 | 7 | |
| α-helix | 1092-1104 | 13 | |
| α-helix | 1107-1110 | 4 | |
| α-helix | 1114-1120 | 7 | |
| α-helix | 1125-1133 | 9 | |
| α-helix | 1136-1140 | 5 | |
| α-helix | 1144-1154 | 11 | |
| α-helix | 359-390 | 32 | |
| α-helix | 397-421 | 25 | |
| α-helix | 423-433 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-5 | 4 | 3 |
| β-strand | 6 | 1 | 4 |
| β-strand | 13-16 | 4 | 3 |
| α-helix | 17-18 | 2 | |
| β-strand | 23-30 | 8 | 4 |
| β-strand | 36-43 | 8 | 4 |
| α-helix | 46-48 | 3 | |
| β-strand | 54-58 | 5 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Muscarinic acetylcholine receptor M1,Endolysin fusion | A | protein | 499 | Homo sapiens, Enterobacteria phage T4 | D9IEF7, P11229 (AlphaFold model) |
| Muscarinic toxin 7 | C | protein | 69 | Dendroaspis angusticeps | Q8QGR0 (AlphaFold model) |
>6WJC_1 Muscarinic acetylcholine receptor M1,Endolysin fusion (chains A) DYKDDDDAAAQTSAPPAVSPQITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFK VNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASQA RVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGER TVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRNIFEMLRIDEGLR LKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAA VRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLA KSRWYNQTPNRAKRVITTFRTGTWDAYFSLVKEKKAARTLSAILLAFILTWTPYNIMVLV STFCKDCVPETLWELGYWLCYVNSTINPMCYALCNKAFRDTFRLLLLCRWDKRRWRKIPK RPGSVHRTPSRQCHHHHHH
>6WJC_2 Muscarinic toxin 7 (chains C) GPGSLTCVKSNSIWFPTSEDCPDGQNLCFKRWQYISPRMYDFTRGCAATCPKAEYRDVIN CCGTDKCNK
| ID | Name | Formula | Copies |
|---|---|---|---|
| OIN | (1R,5S)-8-methyl-8-AZABICYCLO[3.2.1]OCT-3-yl (2R)-3-hydroxy-2-phenylpropanoate | C17 H23 N O3 | 1 |
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 4 |
| ACM | Acetamide | C2 H5 N O | 1 |
Structure and selectivity engineering of the M1muscarinic receptor toxin complex. Maeda, S., Xu, J., N Kadji, F.M. et al. Science (2020) 369:161-167. DOI 10.1126/science.aax2517 · PubMed
Other PDB entries of the same protein (UniProt D9IEF7), best resolution first:
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