9MBD: Apo-GPCR

Cryo-EM structure of Apo-GPCR. Determined by electron microscopy at 3.32 Å resolution. Released 1 Oct 2025.

Method: Electron microscopy
Resolution: 3.32 Å
Organism: Homo sapiens
Chains: 2
Atoms: 11,935
Mol. weight: 203.72 kDa
Released: 1 Oct 2025

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

Secondary structure: helices and β-sheets

9MBD contains 70 α-helices and 58 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: 34 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	40-41	2	1
β-strand	46-52	7	1
α-helix	73-86	14
β-strand	98-99	2	1
β-strand	101-104	4	1
α-helix	110-119	10
α-helix	143-146	4
β-strand	147-151	5	1
α-helix	156-167	12
β-strand	173	1	1
β-strand	175	1	2
α-helix	181-183	3
β-strand	194	1	2
α-helix	197-198	2
α-helix	199-201	3
α-helix	202-213	12
β-strand	217-218	2	3
β-strand	219-220	2	4
α-helix	226-242	17
β-strand	246-247	2	3
α-helix	257-258	2
α-helix	262-269	8
β-strand	277-279	3	4
α-helix	284-296	13
β-strand	304-306	3	4
α-helix	323-325	3
β-strand	331-333	3	5
α-helix	339-345	7
α-helix	359-365	7
α-helix	400-402	3
α-helix	405-420	16
α-helix	439-446	8
β-strand	451-452	2	6
α-helix	454-456	3
β-strand	458-459	2	6
β-strand	466	1	2
α-helix	467-469	3
β-strand	470-474	5	5
β-strand	487-492	6	5
β-strand	495-497	3	5
α-helix	499-501	3
β-strand	524-528	5	7
α-helix	529	1
β-strand	536-540	5	7
β-strand	545-547	3	8
β-strand	553-555	3	8
α-helix	556-557	2
β-strand	561-562	2	9
β-strand	569-570	2	9
α-helix	571-573	3
β-strand	575	1	10
α-helix	582-584	3
α-helix	585-607	23
α-helix	614-616	3
α-helix	622-639	18
α-helix	649-677	29
α-helix	691-699	9
α-helix	703-711	9
β-strand	724	1	10
β-strand	739	1	10
α-helix	746-769	24
α-helix	780-801	22
α-helix	813-831	19

Chain B: 36 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	40-41	2	11
β-strand	46-52	7	11
α-helix	73-86	14
β-strand	98-99	2	11
β-strand	101-104	4	11
α-helix	110-119	10
α-helix	143-146	4
β-strand	147-151	5	11
α-helix	156-167	12
β-strand	173	1	11
β-strand	175	1	12
α-helix	181-183	3
β-strand	194	1	12
α-helix	197-198	2
α-helix	199-201	3
α-helix	202-213	12
β-strand	217-218	2	13
β-strand	219-220	2	14
α-helix	226-242	17
β-strand	246-247	2	13
α-helix	257-258	2
α-helix	262-269	8
β-strand	277-279	3	14
α-helix	284-296	13
β-strand	304-306	3	14
α-helix	323-325	3
β-strand	331-333	3	15
α-helix	339-345	7
α-helix	359-365	7
α-helix	400-402	3
α-helix	405-420	16
α-helix	439-446	8
β-strand	451-452	2	16
α-helix	454-456	3
β-strand	458-459	2	16
β-strand	466	1	12
α-helix	467-469	3
β-strand	470-474	5	15
β-strand	487-492	6	15
β-strand	495-497	3	15
α-helix	499-501	3
β-strand	524-528	5	17
α-helix	529	1
β-strand	536-540	5	17
β-strand	545-547	3	18
β-strand	553-555	3	18
α-helix	556-557	2
β-strand	561-562	2	19
β-strand	569-570	2	19
α-helix	571-573	3
β-strand	575	1	20
α-helix	582-584	3
α-helix	585-607	23
α-helix	614-616	3
α-helix	622-639	18
α-helix	649-677	29
α-helix	691-699	9
α-helix	703-711	9
α-helix	717	1
α-helix	719	1
β-strand	724	1	20
β-strand	739	1	20
α-helix	746-769	24
α-helix	780-801	22
α-helix	813-831	19

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

>9MBD_1 Metabotropic glutamate receptor 8 (chains A, B)
MVCEGKRSASCPCFFLLTAKFYWILTMMQRTHSQEYAHSIRVDGDIILGGLFPVHAKGER
GVPCGELKKEKGIHRLEAMLYAIDQINKDPDLLSNITLGVRILDTCSRDTYALEQSLTFV
QALIEKDASDVKCANGDPPIFTKPDKISGVIGAAASSVSIMVANILRLFKIPQISYASTA
PELSDNTRYDFFSRVVPPDSYQAQAMVDIVTALGWNYVSTLASEGNYGESGVEAFTQISR
EIGGVCIAQSQKIPREPRPGEFEKIIKRLLETPNARAVIMFANEDDIRRILEAAKKLNQS
GHFLWIGSDSWGSKIAPVYQQEEIAEGAVTILPKRASIDGFDRYFRSRTLANNRRNVWFA
EFWEENFGCKLGSHGKRNSHIKKCTGLERIARDSSYEQEGKVQFVIDAVYSMAYALHNMH
KDLCPGYIGLCPRMSTIDGKELLGYIRAVNFNGSAGTPVTFNENGDAPGRYDIFQYQITN
KSTEYKVIGHWTNQLHLKVEDMQWAHREHTHPASVCSLPCKPGERKKTVKGVPCCWHCER
CEGYNYQVDELSCELCPLDQRPNMNRTGCQLIPIIKLEWHSPWAVVPVFVAILGIIATTF
VIVTFVRYNDTPIVRASGRELSYVLLTGIFLCYSITFLMIAAPDTIICSFRRVFLGLGMC
FSYAALLTKTNRIHRIFEQGKKSVTAPKFISPASQLVITFSLISVQLLGVFVWFVVDPPH
IIIDYGEQRTLDPEKARGVLKCDISDLSLICSLGYSILLMVTCTVYAIKTRGVPETFNEA
KPIGFTMYTTCIIWLAFIPIFFGTAQSAEKMYIQTTTLTVSMSLSASVSLGMLYMPKVYI
IIFHPEQNVQKRKRSFKAVVTAATMQSKLIQKGNDRPNGEVKSELCESLETNTSSTKTTY
ISYSNHSI

Primary citation

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:

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
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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