Cryo-EM structure of LY2794193-bound mGlu3. Determined by electron microscopy at 3.68 Å resolution. Released 16 Mar 2022.
Explore 7WIH in 3D Show helices and sheets RCSB PDB PDBe
7WIH contains 70 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 | 33-34 | 2 | 1 |
| β-strand | 39-41 | 3 | 2 |
| β-strand | 44-45 | 2 | 3 |
| α-helix | 66-77 | 12 | |
| β-strand | 91-93 | 3 | 2 |
| β-strand | 94-95 | 2 | 1 |
| β-strand | 96-97 | 2 | 3 |
| α-helix | 102-113 | 12 | |
| β-strand | 145 | 1 | 4 |
| α-helix | 152-155 | 4 | |
| β-strand | 168 | 1 | 4 |
| α-helix | 177-179 | 3 | |
| β-strand | 187 | 1 | 4 |
| α-helix | 195-202 | 8 | |
| β-strand | 212-213 | 2 | 5 |
| β-strand | 214-217 | 4 | 6 |
| α-helix | 231-234 | 4 | |
| β-strand | 240-241 | 2 | 5 |
| β-strand | 245-246 | 2 | 6 |
| α-helix | 257-260 | 4 | |
| α-helix | 262-265 | 4 | |
| β-strand | 271-274 | 4 | 6 |
| β-strand | 296-299 | 4 | 6 |
| β-strand | 321-322 | 2 | 6 |
| α-helix | 337-339 | 3 | |
| α-helix | 354-358 | 5 | |
| α-helix | 371-374 | 4 | |
| α-helix | 388-390 | 3 | |
| α-helix | 391-406 | 16 | |
| α-helix | 408-411 | 4 | |
| α-helix | 427-430 | 4 | |
| β-strand | 469-470 | 2 | 7 |
| β-strand | 481-482 | 2 | 7 |
| α-helix | 500-502 | 3 | |
| β-strand | 538-539 | 2 | 8 |
| β-strand | 547-548 | 2 | 8 |
| β-strand | 553-555 | 3 | 9 |
| β-strand | 562-564 | 3 | 9 |
| α-helix | 579-585 | 7 | |
| α-helix | 588-593 | 6 | |
| α-helix | 595 | 1 | |
| α-helix | 596-600 | 5 | |
| α-helix | 605-608 | 4 | |
| α-helix | 615-618 | 4 | |
| α-helix | 620-625 | 6 | |
| α-helix | 641-651 | 11 | |
| α-helix | 661-665 | 5 | |
| α-helix | 691-695 | 5 | |
| α-helix | 702-708 | 7 | |
| α-helix | 734-749 | 16 | |
| α-helix | 751-754 | 4 | |
| α-helix | 767-771 | 5 | |
| α-helix | 772-773 | 2 | |
| α-helix | 774-778 | 5 | |
| α-helix | 779-782 | 4 | |
| α-helix | 786-788 | 3 | |
| α-helix | 800-812 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Metabotropic glutamate receptor 3 | A, B | protein | 887 | Homo sapiens | Q14832 (AlphaFold model) |
>7WIH_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 |
| CWY | (1S,2S,4S,5R,6S)-2-amino-4-[(3-methoxybenzene-1-carbonyl)amino]bicyclo[3.1.0]he… | C16 H18 N2 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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