9N8Z: Cryo EM Structure of Full Length mGluR8

Cryo EM Structure of Full Length mGluR8 Bound to Agonist L-AP4 and PAM VU6005649, class 2. Determined by electron microscopy at 2.97 Å resolution. Released 9 Sept 2026.

Method: Electron microscopy
Resolution: 2.97 Å
Organism: Homo sapiens
Chains: 2
Atoms: 10,501
Mol. weight: 202.84 kDa
Ligands: E7P, A1BWG
Released: 9 Sept 2026

Explore 9N8Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9N8Z contains 71 α-helices and 60 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: 33 helices, 33 β-strands

Element	Residues	Length	Sheet
β-strand	40-42	3	1
β-strand	46-52	7	1
β-strand	55	1	2
β-strand	67	1	2
α-helix	68	1
α-helix	74-88	15
β-strand	98-104	7	1
α-helix	109-120	12
β-strand	147-151	5	1
α-helix	156-169	14
β-strand	173-175	3	1
α-helix	181-184	4
β-strand	192-194	3	1
α-helix	199-212	14
β-strand	217-220	4	3
β-strand	222	1	4
β-strand	223	1	5
α-helix	225-242	18
β-strand	246-250	5	3
β-strand	253	1	5
α-helix	257-258	2
α-helix	261-267	7
β-strand	277-278	2	3
β-strand	279	1	6
β-strand	281	1	4
α-helix	284-297	14
β-strand	306	1	6
β-strand	330	1	7
β-strand	333	1	8
α-helix	339-347	9
α-helix	359-366	8
β-strand	370	1	9
α-helix	382	1
β-strand	383	1	9
α-helix	384	1
β-strand	390	1	10
β-strand	394	1	10
α-helix	402-423	22
α-helix	432-434	3
α-helix	439-448	10
β-strand	451-452	2	11
β-strand	458-459	2	11
β-strand	466	1	1
α-helix	467-468	2
β-strand	471	1	8
β-strand	474	1	7
β-strand	487	1	7
α-helix	518-521	4
β-strand	545-546	2	12
β-strand	554-555	2	12
α-helix	556-557	2
β-strand	560-562	3	13
β-strand	569-571	3	13
α-helix	572-573	2
α-helix	585-608	24
α-helix	612-615	4
α-helix	619-640	22
α-helix	647-655	9
α-helix	657-674	18
α-helix	692-716	25
α-helix	723-726	4
α-helix	746-769	24
α-helix	780-795	16
α-helix	797-802	6
α-helix	810-833	24
α-helix	835-843	9

Chain B: 38 helices, 27 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	109-116	8
α-helix	117-120	4
β-strand	147-152	6	14
α-helix	156-169	14
β-strand	173-175	3	14
α-helix	181-183	3
β-strand	192-194	3	14
α-helix	199-212	14
β-strand	217-223	7	16
α-helix	226-242	17
β-strand	246-247	2	16
β-strand	251-253	3	16
α-helix	257-258	2
α-helix	261-270	10
β-strand	277-281	5	16
α-helix	284-296	13
β-strand	304-306	3	16
α-helix	316-318	3
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	375-378	4
α-helix	382	1
β-strand	383	1	17
α-helix	384	1
α-helix	402-423	22
α-helix	432-435	4
α-helix	439-447	9
β-strand	450-452	3	18
β-strand	458-460	3	18
β-strand	470-478	9	16
β-strand	483-492	10	16
β-strand	495	1	16
α-helix	519-521	3
β-strand	524-528	5	19
α-helix	529	1
β-strand	536-540	5	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
α-helix	572-574	3
α-helix	585-604	20
α-helix	621-633	13
α-helix	635-640	6
α-helix	645-653	9
α-helix	657-672	16
α-helix	691-713	23
α-helix	722-726	5
α-helix	746-752	7
α-helix	754-769	16
α-helix	780-795	16
α-helix	797-803	7
α-helix	810-829	20
α-helix	838-843	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Metabotropic glutamate receptor 8	A, B	protein	901	Homo sapiens	O00222 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9N8Z_1 Metabotropic glutamate receptor 8 (chains A, B)
MKTIIALSYIFCLVFADYKDDDDAAAQEYAHSIRVDGDIILGGLFPVHAKGERGVPCGEL
KKEKGIHRLEAMLYAIDQINKDPDLLSNITLGVRILDTCSRDTYALEQSLTFVQALIEKD
ASDVKCANGDPPIFTKPDKISGVIGAAASSVSIMVANILRLFKIPQISYASTAPELSDNT
RYDFFSRVVPPDSYQAQAMVDIVTALGWNYVSTLASEGNYGESGVEAFTQISREIGGVCI
AQSQKIPREPRPGEFEKIIKRLLETPNARAVIMFANEDDIRRILEAAKKLNQSGHFLWIG
SDSWGSKIAPVYQQEEIAEGAVTILPKRASIDGFDRYFRSRTLANNRRNVWFAEFWEENF
GCKLGSHGKRNSHIKKCTGLERIARDSSYEQEGKVQFVIDAVYSMAYALHNMHKDLCPGY
IGLCPRMSTIDGKELLGYIRAVNFNGSAGTPVTFNENGDAPGRYDIFQYQITNKSTEYKV
IGHWTNQLHLKVEDMQWAHREHTHPASVCSLPCKPGERKKTVKGVPCCWHCERCEGYNYQ
VDELSCELCPLDQRPNMNRTGCQLIPIIKLEWHSPWAVVPVFVAILGIIATTFVIVTFVR
YNDTPIVRASGRELSYVLLTGIFLCYSITFLMIAAPDTIICSFRRVFLGLGMCFSYAALL
TKTNRIHRIFEQGKKSVTAPKFISPASQLVITFSLISVQLLGVFVWFVVDPPHIIIDYGE
QRTLDPEKARGVLKCDISDLSLICSLGYSILLMVTCTVYAIKTRGVPETFNEAKPIGFTM
YTTCIIWLAFIPIFFGTAQSAEKMYIQTTTLTVSMSLSASVSLGMLYMPKVYIIIFHPEQ
NVQKRKRSFKAVVTAATMQSKLIQKGNDRPNGEVKSELCESLETNTSSTKTTYISYSNHS
I

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	2

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
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
9Y1M 3.32 Å, Cryo EM Structure of Full Length mGluR8 in Complex with Beta-Arrestin-1 Bound to Agonist…
9Y1N 6.18 Å, Cryo EM Structure of Full lengthmGluR8 Bound to Agonist L-AP4 and PAM VU6005649 in…

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