9Y1M: Cryo EM Structure of Full Length mGluR8

Cryo EM Structure of Full Length mGluR8 in Complex with Beta-Arrestin-1 Bound to Agonist L-AP4 and PAM VU6005649. Determined by electron microscopy at 3.32 Å resolution. Released 30 Sept 2026.

Method: Electron microscopy
Resolution: 3.32 Å
Organism: Homo sapiens
Chains: 2
Atoms: 11,076
Mol. weight: 204.44 kDa
Ligands: E7P, A1BWG
Released: 30 Sept 2026

Explore 9Y1M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Y1M 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.

Chain A: 30 helices, 34 β-strands

Element	Residues	Length	Sheet
β-strand	40-41	2	1
β-strand	46-52	7	1
β-strand	55	1	2
β-strand	67	1	2
α-helix	74-88	15
β-strand	98-104	7	1
α-helix	109-119	11
β-strand	147-152	6	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	217-223	7	3
α-helix	225-242	18
β-strand	246-253	8	3
α-helix	254	1
α-helix	259-270	12
β-strand	277-280	4	3
α-helix	286-296	11
β-strand	306	1	3
α-helix	318-321	4
β-strand	327-329	3	4
β-strand	332-333	2	5
α-helix	340-347	8
α-helix	359-366	8
α-helix	388-389	2
β-strand	390	1	6
β-strand	394	1	6
α-helix	402-423	22
α-helix	432-434	3
α-helix	439-446	8
β-strand	451-452	2	7
β-strand	458-459	2	7
α-helix	466-469	4
β-strand	471-473	3	5
β-strand	475-476	2	4
β-strand	477	1	8
β-strand	484	1	8
β-strand	489-491	3	5
β-strand	495	1	5
α-helix	499-501	3
α-helix	505-507	3
β-strand	524-528	5	9
α-helix	529	1
β-strand	536-540	5	9
β-strand	545-546	2	10
β-strand	554-555	2	10
α-helix	556-557	2
β-strand	560-562	3	11
β-strand	569-571	3	11
α-helix	572-573	2
β-strand	574-575	2	12
α-helix	586-607	22
α-helix	619-639	21
α-helix	645-676	32
α-helix	692-716	25
β-strand	722-723	2	13
β-strand	738-739	2	12
β-strand	740-741	2	13
α-helix	746-770	25
α-helix	780-803	24
α-helix	810-832	23
α-helix	835-841	7

Chain B: 34 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	40-42	3	14
β-strand	46-52	7	14
β-strand	55	1	15
β-strand	67	1	15
α-helix	69-74	6
α-helix	75-88	14
β-strand	98-104	7	14
α-helix	109-121	13
β-strand	147-150	4	14
α-helix	156-167	12
β-strand	173-175	3	14
α-helix	181-184	4
β-strand	192-194	3	14
α-helix	199-212	14
β-strand	217-223	7	16
α-helix	226-242	17
β-strand	246-253	8	16
α-helix	257-258	2
α-helix	261-271	11
β-strand	277-281	5	16
α-helix	284-296	13
β-strand	304-306	3	16
α-helix	322-325	4
β-strand	329-333	5	16
α-helix	339-347	9
α-helix	359-367	9
β-strand	370	1	17
α-helix	373-375	3
α-helix	382	1
β-strand	383	1	17
α-helix	384	1
α-helix	402-423	22
α-helix	439-446	8
β-strand	450-452	3	18
β-strand	458-460	3	18
β-strand	471-477	7	16
β-strand	484-491	8	16
β-strand	495	1	16
α-helix	499-501	3
α-helix	505-507	3
α-helix	518-521	4
β-strand	524-529	6	19
β-strand	532-540	9	19
β-strand	545-547	3	20
β-strand	553-555	3	20
α-helix	556-557	2
β-strand	560-562	3	21
β-strand	569-571	3	21
β-strand	574-575	2	22
α-helix	582-607	26
α-helix	612-617	6
α-helix	621-640	20
α-helix	645-653	9
α-helix	657-682	26
α-helix	692-716	25
β-strand	721-723	3	23
β-strand	738-739	2	22
β-strand	740-742	3	23
α-helix	746-770	25
α-helix	775-777	3
α-helix	780-803	24
α-helix	811-833	23
α-helix	835-842	8
α-helix	845-848	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Metabotropic glutamate receptor 8	A, B	protein	908	Homo sapiens	O00222 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9Y1M_1 Metabotropic glutamate receptor 8 (chains A, B)
MVCEGKRSASCPCFFLLTAKFYWILTMMQRTHSQEYAHSIRVDGDIILGGLFPVHAKGER
GVPCGELKKEKGIHRLEAMLYAIDQINKDPDLLSNITLGVRILDTCSRDTYALEQSLTFV
QALIEKDASDVKCANGDPPIFTKPDKISGVIGAAASSVSIMVANILRLFKIPQISYASTA
PELSDNTRYDFFSRVVPPDSYQAQAMVDIVTALGWNYVSTLASEGNYGESGVEAFTQISR
EIGGVCIAQSQKIPREPRPGEFEKIIKRLLETPNARAVIMFANEDDIRRILEAAKKLNQS
GHFLWIGSDSWGSKIAPVYQQEEIAEGAVTILPKRASIDGFDRYFRSRTLANNRRNVWFA
EFWEENFGCKLGSHGKRNSHIKKCTGLERIARDSSYEQEGKVQFVIDAVYSMAYALHNMH
KDLCPGYIGLCPRMSTIDGKELLGYIRAVNFNGSAGTPVTFNENGDAPGRYDIFQYQITN
KSTEYKVIGHWTNQLHLKVEDMQWAHREHTHPASVCSLPCKPGERKKTVKGVPCCWHCER
CEGYNYQVDELSCELCPLDQRPNMNRTGCQLIPIIKLEWHSPWAVVPVFVAILGIIATTF
VIVTFVRYNDTPIVRASGRELSYVLLTGIFLCYSITFLMIAAPDTIICSFRRVFLGLGMC
FSYAALLTKTNRIHRIFEQGKKSVTAPKFISPASQLVITFSLISVQLLGVFVWFVVDPPH
IIIDYGEQRTLDPEKARGVLKCDISDLSLICSLGYSILLMVTCTVYAIKTRGVPETFNEA
KPIGFTMYTTCIIWLAFIPIFFGTAQSAEKMYIQTTTLTVSMSLSASVSLGMLYMPKVYI
IIFHPEQNVQKRKRSFKAVVTAATMQSKLIQKGNDRPNGEVKSELCESLETNTSSTKTTY
ISYSNHSI

Ligands and cofactors

ID	Name	Formula	Copies
E7P	(2S)-2-amino-4-phosphonobutanoic acid	C4 H10 N O5 P	2
A1BWG	(3P,8S)-3-(2,3-difluoro-4-methoxyphenyl)-2,5-dimethyl-7-(trifluoromethyl)pyrazo…	C16 H12 F5 N3 O	1

Primary citation

Structural basis of active state coupling of metabotropic glutamate receptor 8 to beta-arrestins. Marx, D.C., Huynh, K., Gonzalez-Hernandez, A.J. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-77556-3 · PubMed

Other PDB entries of the same protein (UniProt O00222 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6BSZ 2.65 Å, Human mGlu8 Receptor complexed with glutamate
9N8Y 2.76 Å, Cryo EM Structure of Full Length mGluR8 Bound to Agonist L-AP4 and PAM VU6005649
6BT5 2.92 Å, Human mGlu8 Receptor complexed with L-AP4
6E5V 2.95 Å, human mGlu8 receptor amino terminal domain in complex with…
9MB9 2.97 Å, Cryo-EM structure of Gi-bound GPCR
9MBC 2.97 Å, Cryo-EM structure of agonist-bound GPCR
9N8Z 2.97 Å, Cryo EM Structure of Full Length mGluR8 Bound to Agonist L-AP4 and PAM VU6005649, class 2
9MBA 3.14 Å, Cryo-EM structure of complex of transducer-bound GPCR
9MBB 3.25 Å, Cryo-EM structure of antagonist-bound GPCR
9MBD 3.32 Å, Cryo-EM structure of Apo-GPCR
9Y1N 6.18 Å, Cryo EM Structure of Full lengthmGluR8 Bound to Agonist L-AP4 and PAM VU6005649 in…

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