Cryo-EM structure of LY341495/NAM-bound mGlu3. Determined by electron microscopy at 3.71 Å resolution. Released 16 Mar 2022.
Explore 7WI6 in 3D Show helices and sheets RCSB PDB PDBe
7WI6 contains 70 α-helices and 50 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 | 33-35 | 3 | 1 |
| β-strand | 39-45 | 7 | 1 |
| α-helix | 66-79 | 14 | |
| β-strand | 91-97 | 7 | 1 |
| α-helix | 102-113 | 12 | |
| β-strand | 145-146 | 2 | 1 |
| β-strand | 168-169 | 2 | 1 |
| α-helix | 177-179 | 3 | |
| β-strand | 187 | 1 | 1 |
| β-strand | 189 | 1 | 2 |
| β-strand | 212-218 | 7 | 3 |
| α-helix | 227-229 | 3 | |
| α-helix | 231-233 | 3 | |
| α-helix | 235-237 | 3 | |
| β-strand | 240-247 | 8 | 3 |
| β-strand | 271-274 | 4 | 3 |
| β-strand | 296-299 | 4 | 3 |
| β-strand | 321-325 | 5 | 3 |
| α-helix | 328-330 | 3 | |
| α-helix | 331-337 | 7 | |
| α-helix | 351-354 | 4 | |
| α-helix | 400-408 | 9 | |
| α-helix | 420-422 | 3 | |
| α-helix | 427-434 | 8 | |
| β-strand | 441 | 1 | 4 |
| α-helix | 442 | 1 | |
| β-strand | 453 | 1 | 4 |
| β-strand | 461 | 1 | 2 |
| α-helix | 462-464 | 3 | |
| β-strand | 466-470 | 5 | 3 |
| β-strand | 481-482 | 2 | 3 |
| β-strand | 484-485 | 2 | 5 |
| β-strand | 491-492 | 2 | 5 |
| α-helix | 515-517 | 3 | |
| β-strand | 521 | 1 | 6 |
| β-strand | 530 | 1 | 6 |
| β-strand | 538-542 | 5 | 7 |
| β-strand | 545-548 | 4 | 7 |
| α-helix | 578-587 | 10 | |
| α-helix | 591-597 | 7 | |
| α-helix | 605-607 | 3 | |
| α-helix | 616-624 | 9 | |
| α-helix | 625-627 | 3 | |
| α-helix | 629-631 | 3 | |
| α-helix | 640-645 | 6 | |
| α-helix | 650-653 | 4 | |
| α-helix | 658-660 | 3 | |
| α-helix | 662-664 | 3 | |
| α-helix | 692-698 | 7 | |
| α-helix | 704-708 | 5 | |
| β-strand | 718-720 | 3 | 8 |
| β-strand | 726-728 | 3 | 8 |
| α-helix | 734-741 | 8 | |
| α-helix | 744-750 | 7 | |
| α-helix | 773-775 | 3 | |
| α-helix | 780-783 | 4 | |
| α-helix | 787-791 | 5 | |
| α-helix | 798-801 | 4 | |
| α-helix | 804-810 | 7 | |
| α-helix | 817-819 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Metabotropic glutamate receptor 3 | A, B | protein | 887 | Homo sapiens | Q14832 (AlphaFold model) |
>7WI6_1 Metabotropic glutamate receptor 3 (chains A, B) MKTIIALSYIFCLVFADYKDDDDENLYFQGLGDHNFLRREIKIEGDLVLGGLFPINEKGT GTEECGRINEDRGIQRLEAMLFAIDEINKDDYLLPGVKLGVHILDTCSRDTYALEQSLEF VRASLTKVDEAEYMCPDGSYAIQENIPLLIAGVIGGSYSSVSIQVANLLRLFQIPQISYA STSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQ EARLRNICIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAASRAN ASFTWVASDGWGAQESIIKGSEHVAYGAITLELASQPVRQFDRYFQSLNPYNNHRNPWFR DFWEQKFQCSLQNKRNHRRVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTLC PNTTKLCDAMKILDGKKLYKDYLLKINFTAPFNPNKDADSIVKFDTFGDGMGRYNVFNFQ NVGGKYSYLKVGHWAETLSLDVNSIHWSRNSVPTSQCSDPCAPNEMKNMQPGDVCCWICI PCEPYEYLADEFTCMDCGSGQWPTADLTGCYDLPEDYIRWEDAWAIGPVTIACLGFMCTC MVVTVFIKHNNTPLVKASGRELCYILLFGVGLSYCMTFFFIAKPSPVICALRRLGLGSSF AICYSALLTKTNCIARIFDGVKNGAQRPKFISPSSQVFICLGLILVQIVMVSVWLILEAP GTRRYTLAEKRETVILKCNVKDSSMLISLTYDVILVILCTVYAFKTRKCPENFNEAKFIG FTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCISVSLSGFVVLGCLFAPKVHIILFQPQK NVVTHRLHLNRFSVSGTGTTYSQSSASTYVPTVCNGREVLDSTTSSL
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
| Z99 | 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine | C20 H19 N O5 | 2 |
Structural basis of the activation of metabotropic glutamate receptor 3. Fang, W., Yang, F., Xu, C. et al. Cell Res (2022) 32:695-698. DOI 10.1038/s41422-022-00623-z · PubMed
Other PDB entries of the same protein (UniProt Q14832 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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