Cryo-EM structure of inactive mGlu3 bound to LY341495. Determined by electron microscopy at 4.17 Å resolution. Released 16 Mar 2022.
Explore 7WI8 in 3D Show helices and sheets RCSB PDB PDBe
7WI8 contains 76 α-helices and 44 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 | 39-43 | 5 | 1 |
| α-helix | 66-79 | 14 | |
| β-strand | 91-95 | 5 | 1 |
| α-helix | 102-113 | 12 | |
| β-strand | 142-146 | 5 | 1 |
| α-helix | 151-154 | 4 | |
| β-strand | 168-169 | 2 | 1 |
| β-strand | 187 | 1 | 1 |
| β-strand | 189 | 1 | 2 |
| α-helix | 192-193 | 2 | |
| α-helix | 201-203 | 3 | |
| α-helix | 205-208 | 4 | |
| β-strand | 212-217 | 6 | 3 |
| α-helix | 223-231 | 9 | |
| β-strand | 240-246 | 7 | 3 |
| β-strand | 272-274 | 3 | 3 |
| α-helix | 279-281 | 3 | |
| α-helix | 282-285 | 4 | |
| α-helix | 288-291 | 4 | |
| β-strand | 297-299 | 3 | 3 |
| β-strand | 320-325 | 6 | 3 |
| α-helix | 331-337 | 7 | |
| α-helix | 351-359 | 9 | |
| α-helix | 390-396 | 7 | |
| α-helix | 398-405 | 8 | |
| α-helix | 407-411 | 5 | |
| α-helix | 428-434 | 7 | |
| β-strand | 441 | 1 | 4 |
| β-strand | 453 | 1 | 4 |
| β-strand | 461 | 1 | 2 |
| α-helix | 462-464 | 3 | |
| β-strand | 466-470 | 5 | 3 |
| β-strand | 481-486 | 6 | 3 |
| β-strand | 490-492 | 3 | 3 |
| α-helix | 515-517 | 3 | |
| β-strand | 521 | 1 | 5 |
| β-strand | 530 | 1 | 5 |
| β-strand | 538-539 | 2 | 6 |
| β-strand | 547-548 | 2 | 6 |
| α-helix | 553-555 | 3 | |
| α-helix | 579-588 | 10 | |
| α-helix | 590-594 | 5 | |
| α-helix | 615-618 | 4 | |
| α-helix | 621-632 | 12 | |
| α-helix | 638-645 | 8 | |
| α-helix | 648-650 | 3 | |
| α-helix | 652-655 | 4 | |
| α-helix | 657-666 | 10 | |
| α-helix | 689-694 | 6 | |
| α-helix | 696-698 | 3 | |
| α-helix | 699-707 | 9 | |
| α-helix | 734-740 | 7 | |
| α-helix | 742-747 | 6 | |
| α-helix | 750-752 | 3 | |
| α-helix | 753-757 | 5 | |
| α-helix | 772-788 | 17 | |
| α-helix | 796-810 | 15 | |
| α-helix | 811-815 | 5 | |
| α-helix | 816-819 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Metabotropic glutamate receptor 3 | A, B | protein | 887 | Homo sapiens | Q14832 (AlphaFold model) |
>7WI8_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 |
|---|---|---|---|
| Z99 | 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine | C20 H19 N O5 | 2 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 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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