Cryo-EM structure of antagonist-bound GPCR. Determined by electron microscopy at 3.25 Å resolution. Released 1 Oct 2025.
Explore 9MBB in 3D Show helices and sheets RCSB PDB PDBe
9MBB contains 70 α-helices and 56 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 | 56 | 1 | 2 |
| β-strand | 64 | 1 | 2 |
| α-helix | 73-86 | 14 | |
| β-strand | 98-104 | 7 | 1 |
| α-helix | 109-119 | 11 | |
| α-helix | 141-145 | 5 | |
| β-strand | 147-151 | 5 | 1 |
| α-helix | 159-167 | 9 | |
| β-strand | 173-175 | 3 | 1 |
| α-helix | 181-183 | 3 | |
| β-strand | 192-194 | 3 | 1 |
| α-helix | 199-201 | 3 | |
| α-helix | 203-212 | 10 | |
| β-strand | 217-222 | 6 | 3 |
| α-helix | 226-239 | 14 | |
| β-strand | 246-252 | 7 | 3 |
| α-helix | 257-258 | 2 | |
| α-helix | 261-269 | 9 | |
| β-strand | 277-281 | 5 | 3 |
| α-helix | 284-293 | 10 | |
| β-strand | 304-307 | 4 | 3 |
| β-strand | 328-333 | 6 | 3 |
| α-helix | 339-347 | 9 | |
| α-helix | 360-367 | 8 | |
| α-helix | 402-423 | 22 | |
| α-helix | 432-435 | 4 | |
| α-helix | 439-446 | 8 | |
| β-strand | 451-452 | 2 | 4 |
| β-strand | 458-459 | 2 | 4 |
| β-strand | 470-479 | 10 | 3 |
| β-strand | 482-492 | 11 | 3 |
| β-strand | 495-497 | 3 | 3 |
| α-helix | 499-501 | 3 | |
| β-strand | 524-528 | 5 | 5 |
| α-helix | 529 | 1 | |
| β-strand | 536-540 | 5 | 5 |
| β-strand | 545 | 1 | 6 |
| β-strand | 555 | 1 | 6 |
| α-helix | 556-557 | 2 | |
| β-strand | 561-562 | 2 | 7 |
| α-helix | 563 | 1 | |
| β-strand | 569-570 | 2 | 7 |
| α-helix | 571-573 | 3 | |
| β-strand | 574 | 1 | 8 |
| α-helix | 585-607 | 23 | |
| α-helix | 615-618 | 4 | |
| α-helix | 620-638 | 19 | |
| α-helix | 642-643 | 2 | |
| α-helix | 647-674 | 28 | |
| α-helix | 675-677 | 3 | |
| α-helix | 691-711 | 21 | |
| β-strand | 722-723 | 2 | 9 |
| β-strand | 738 | 1 | 8 |
| β-strand | 740-741 | 2 | 9 |
| α-helix | 746-752 | 7 | |
| α-helix | 754-771 | 18 | |
| α-helix | 780-795 | 16 | |
| α-helix | 797-802 | 6 | |
| α-helix | 803-805 | 3 | |
| α-helix | 810-829 | 20 | |
| α-helix | 836-838 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Metabotropic glutamate receptor 8 | A, B | protein | 908 | Homo sapiens | O00222 (AlphaFold model) |
>9MBB_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 |
|---|---|---|---|
| Z99 | 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine | C20 H19 N O5 | 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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