Cryo-EM structure of agonist-bound GPCR. Determined by electron microscopy at 2.97 Å resolution. Released 1 Oct 2025.
Explore 9MBC in 3D Show helices and sheets RCSB PDB PDBe
9MBC contains 64 α-helices and 64 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 | 40-42 | 3 | 1 |
| β-strand | 46-52 | 7 | 1 |
| β-strand | 55-57 | 3 | 2 |
| β-strand | 64-67 | 4 | 2 |
| α-helix | 69-73 | 5 | |
| α-helix | 74-88 | 15 | |
| β-strand | 98-104 | 7 | 1 |
| α-helix | 109-119 | 11 | |
| β-strand | 147-151 | 5 | 1 |
| α-helix | 156-166 | 11 | |
| β-strand | 173-175 | 3 | 1 |
| α-helix | 181-184 | 4 | |
| β-strand | 192-194 | 3 | 1 |
| α-helix | 199-212 | 14 | |
| β-strand | 217-222 | 6 | 3 |
| β-strand | 223 | 1 | 4 |
| α-helix | 227-242 | 16 | |
| β-strand | 246-250 | 5 | 3 |
| β-strand | 253 | 1 | 4 |
| α-helix | 257-258 | 2 | |
| α-helix | 261-269 | 9 | |
| β-strand | 277-281 | 5 | 3 |
| α-helix | 284-296 | 13 | |
| β-strand | 304-307 | 4 | 3 |
| α-helix | 316-318 | 3 | |
| α-helix | 322-325 | 4 | |
| β-strand | 329-333 | 5 | 3 |
| α-helix | 339-346 | 8 | |
| α-helix | 350-352 | 3 | |
| α-helix | 359-367 | 9 | |
| β-strand | 369-370 | 2 | 5 |
| β-strand | 382-383 | 2 | 5 |
| α-helix | 402-423 | 22 | |
| α-helix | 432-434 | 3 | |
| α-helix | 439-446 | 8 | |
| β-strand | 451-452 | 2 | 6 |
| β-strand | 458-459 | 2 | 6 |
| β-strand | 470-479 | 10 | 3 |
| β-strand | 482-492 | 11 | 3 |
| β-strand | 495-497 | 3 | 3 |
| α-helix | 499-501 | 3 | |
| α-helix | 518-520 | 3 | |
| β-strand | 525-528 | 4 | 7 |
| α-helix | 529 | 1 | |
| β-strand | 536-539 | 4 | 7 |
| β-strand | 546-549 | 4 | 8 |
| β-strand | 552-554 | 3 | 8 |
| β-strand | 561-562 | 2 | 9 |
| β-strand | 569-570 | 2 | 9 |
| α-helix | 571-573 | 3 | |
| β-strand | 574-575 | 2 | 10 |
| α-helix | 585-607 | 23 | |
| α-helix | 612-617 | 6 | |
| α-helix | 621-637 | 17 | |
| α-helix | 651-664 | 14 | |
| α-helix | 693-716 | 24 | |
| β-strand | 721-723 | 3 | 11 |
| α-helix | 733-735 | 3 | |
| β-strand | 738-739 | 2 | 10 |
| β-strand | 740-742 | 3 | 11 |
| α-helix | 751-761 | 11 | |
| α-helix | 780-795 | 16 | |
| α-helix | 797-801 | 5 | |
| α-helix | 810-842 | 33 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Metabotropic glutamate receptor 8 | A, B | protein | 908 | Homo sapiens | O00222 (AlphaFold model) |
>9MBC_1 Metabotropic glutamate receptor 8 (chains A, B) MVCEGKRSASCPCFFLLTAKFYWILTMMQRTHSQEYAHSIRVDGDIILGGLFPVHAKGER GVPCGELKKEKGIHRLEAMLYAIDQINKDPDLLSNITLGVRILDTCSRDTYALEQSLTFV QALIEKDASDVKCANGDPPIFTKPDKISGVIGAAASSVSIMVANILRLFKIPQISYASTA PELSDNTRYDFFSRVVPPDSYQAQAMVDIVTALGWNYVSTLASEGNYGESGVEAFTQISR EIGGVCIAQSQKIPREPRPGEFEKIIKRLLETPNARAVIMFANEDDIRRILEAAKKLNQS GHFLWIGSDSWGSKIAPVYQQEEIAEGAVTILPKRASIDGFDRYFRSRTLANNRRNVWFA EFWEENFGCKLGSHGKRNSHIKKCTGLERIARDSSYEQEGKVQFVIDAVYSMAYALHNMH KDLCPGYIGLCPRMSTIDGKELLGYIRAVNFNGSAGTPVTFNENGDAPGRYDIFQYQITN KSTEYKVIGHWTNQLHLKVEDMQWAHREHTHPASVCSLPCKPGERKKTVKGVPCCWHCER CEGYNYQVDELSCELCPLDQRPNMNRTGCQLIPIIKLEWHSPWAVVPVFVAILGIIATTF VIVTFVRYNDTPIVRASGRELSYVLLTGIFLCYSITFLMIAAPDTIICSFRRVFLGLGMC FSYAALLTKTNRIHRIFEQGKKSVTAPKFISPASQLVITFSLISVQLLGVFVWFVVDPPH IIIDYGEQRTLDPEKARGVLKCDISDLSLICSLGYSILLMVTCTVYAIKTRGVPETFNEA KPIGFTMYTTCIIWLAFIPIFFGTAQSAEKMYIQTTTLTVSMSLSASVSLGMLYMPKVYI IIFHPEQNVQKRKRSFKAVVTAATMQSKLIQKGNDRPNGEVKSELCESLETNTSSTKTTY ISYSNHSI
| ID | Name | Formula | Copies |
|---|---|---|---|
| HVG | 4-[(S)-amino(carboxy)methyl]benzene-1,2-dicarboxylic acid | C10 H9 N O6 | 2 |
| A1ENR | 2-[(4-bromophenyl)methylsulfanyl]-~{N}-[4-[(2~{S})-butan-2-yl]phenyl]ethanamide | C19 H22 Br N O S | 2 |
Structural characterization of five functional states of metabotropic glutamate receptor 8. Zhao, J., Deng, Y., Xu, Z. et al. Mol Cell (2025) 85:3460-3473.e6. DOI 10.1016/j.molcel.2025.08.019 · PubMed
Other PDB entries of the same protein (UniProt O00222 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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