Structural mechanism of CB1R binding to peripheral and biased inverse agonists. Determined by electron microscopy at 3.3 Å resolution. Released 20 Nov 2024.
Explore 9B9Z in 3D Show helices and sheets RCSB PDB PDBe
9B9Z contains 26 α-helices and 23 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 |
|---|---|---|---|
| β-strand | 3-7 | 5 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 17-25 | 9 | 1 |
| β-strand | 33-39 | 7 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 58-59 | 2 | 2 |
| β-strand | 67-72 | 6 | 1 |
| β-strand | 77-83 | 7 | 1 |
| β-strand | 91-100 | 10 | 2 |
| β-strand | 108-112 | 5 | 2 |
| β-strand | 116-121 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 113-142 | 30 | |
| α-helix | 145-148 | 4 | |
| α-helix | 151-153 | 3 | |
| α-helix | 154-174 | 21 | |
| α-helix | 175-179 | 5 | |
| α-helix | 182-184 | 3 | |
| α-helix | 186-219 | 34 | |
| α-helix | 221-227 | 7 | |
| α-helix | 230-249 | 20 | |
| α-helix | 250-253 | 4 | |
| α-helix | 257-260 | 4 | |
| β-strand | 264 | 1 | 3 |
| β-strand | 272 | 1 | 3 |
| α-helix | 273-1004 | 33 | |
| α-helix | 1009-1011 | 3 | |
| α-helix | 1016-1026 | 11 | |
| β-strand | 1033-1038 | 6 | 4 |
| β-strand | 1041 | 1 | 5 |
| β-strand | 1046 | 1 | 6 |
| α-helix | 1048-1058 | 11 | |
| α-helix | 1064-1066 | 3 | |
| β-strand | 1067-1072 | 6 | 4 |
| β-strand | 1075 | 1 | 5 |
| α-helix | 1077-1089 | 13 | |
| β-strand | 1093-1096 | 4 | 4 |
| α-helix | 1102-1109 | 8 | |
| β-strand | 1114-1117 | 4 | 4 |
| β-strand | 1119 | 1 | 6 |
| α-helix | 1126-1133 | 8 | |
| β-strand | 1137-1141 | 5 | 4 |
| α-helix | 1144-1146 | 3 | |
| β-strand | 1156-1158 | 3 | 4 |
| α-helix | 1163-1176 | 14 | |
| α-helix | 1182-1193 | 12 | |
| α-helix | 333-367 | 35 | |
| α-helix | 373-382 | 10 | |
| α-helix | 385-400 | 16 | |
| α-helix | 402-408 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CNb36 | N | protein | 128 | Lama glama | |
| Cannabinoid receptor 1,Glycogen synthase | R | protein | 535 | Homo sapiens, Pyrococcus abyssi GE5 | P21554 (AlphaFold model), Q9V2J8 (AlphaFold model) |
>9B9Z_1 CNb36 (chains N) QVQLQESGGGLVQAGGSLRLSCAASGTIFGPDVMGWYRQAPGKERELVAGISNGANTYYA DSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCAAEVLDYTFAYLYHAYWGQGTQVTV SSHHHHHH
>9B9Z_2 Cannabinoid receptor 1,Glycogen synthase (chains R) DYKDDDDAMDQVNITEFYNKSLSSFENLYFQGGIQCGENFMDIECFMVLNPSQQLAIAVL SLTLGTFTVLENLLVLCVILHSRSLRCRPSYHFIGSLAVADLLGSVIFVYSFIDFHVFHR KDSRNVFLFKLGGVTASFTAKVGSLFLAAIDRYISIHRPLAYKRIVTRPKAVVAFCLMWT IAIVIAVLPLLGWNCEKLQSVCSDIFPHIDKTYLMFWIGVVSVLLLFIVYAYMYILWKAG IDCSFWNESYLTGSRDERKKSLLSKFGMDEGVTFMFIGRFDRGQKGVDVLLKAIEILSSK KEFQEMRFIIIGKGDPELEGWARSLEEKHGNVKVITEMLSREFVRELYGSVDFVIIPSYF EPFGLVALEAMCLGAIPIASAVGGLRDIITNETGILVKAGDPGELANAILKALELSRSDL SKFRENCKKRAMSFSDQARMDIELAKTLVLILVVLIICWGPLLAIMVYDVFGKMNKLIKT VFAFCSMLCLLNSTVNPIIYALRSKDLRHAFRSMFPSCENLYFQGHHHHHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1AKO | (4S)-3-(4-chlorophenyl)-N'-[(1E)-ethanimidoyl]-4-phenyl-N-[4-(trifluoromethyl)b… | C25 H21 Cl F3 N5 O2 S | 1 |
Structural mechanism of CB 1 R binding to peripheral and biased inverse agonists. Kumari, P., Dvoracsko, S., Enos, M.D. et al. Nat Commun (2024) 15:10694-10694. DOI 10.1038/s41467-024-54206-0 · PubMed
Other PDB entries of the same protein (UniProt P21554 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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