8X0G: Metabotropic glutamate receptor 5

Human FL Metabotropic glutamate receptor 5, mGlu5-5M with quisqualate, Acc conformation (purified with PAM VU0409551 but not modelled). Determined by electron microscopy at 3.0 Å resolution. Released 6 Nov 2024.

Method: Electron microscopy
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 12,129
Mol. weight: 188.2 kDa
Ligands: QUS, NAG
Released: 6 Nov 2024

Explore 8X0G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8X0G contains 68 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: 37 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	29-31	3	1
β-strand	35-41	7	1
β-strand	44	1	2
α-helix	45-48	4
β-strand	60	1	2
α-helix	62-67	6
α-helix	68-80	13
β-strand	91-97	7	1
α-helix	102-113	12
α-helix	114-116	3
β-strand	143-147	5	1
α-helix	152-162	11
α-helix	163-165	3
β-strand	169-171	3	1
α-helix	177-180	4
β-strand	188-190	3	1
α-helix	195-208	14
β-strand	213-219	7	3
α-helix	223-236	14
β-strand	241-248	8	3
α-helix	254-264	11
α-helix	265-267	3
β-strand	273-277	5	3
α-helix	280-293	14
β-strand	300-302	3	3
α-helix	318-321	4
β-strand	325-329	5	3
α-helix	332-334	3
α-helix	335-341	7
α-helix	355-362	8
β-strand	366	1	4
β-strand	380	1	4
α-helix	397-418	22
α-helix	427-429	3
α-helix	434-442	9
β-strand	445-447	3	5
β-strand	453-455	3	5
β-strand	466-475	10	3
β-strand	478-488	11	3
β-strand	491-494	4	3
α-helix	507-508	2
β-strand	520-524	5	6
β-strand	532-536	5	6
α-helix	537-538	2
β-strand	541-543	3	7
β-strand	549-551	3	7
β-strand	557-558	2	8
α-helix	560-562	3
β-strand	565-566	2	8
α-helix	567-570	4
β-strand	571	1	9
α-helix	578-603	26
α-helix	608-610	3
α-helix	615-631	17
α-helix	632-634	3
α-helix	641-644	4
α-helix	647-671	25
α-helix	690-692	3
α-helix	693-714	22
β-strand	719-722	4	9
β-strand	730-733	4	9
α-helix	738-761	24
α-helix	767-769	3
α-helix	770-793	24
α-helix	798-815	18
α-helix	819-826	8

Chain B: 31 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	29-31	3	10
β-strand	35-41	7	10
β-strand	44	1	11
α-helix	45-48	4
β-strand	60	1	11
α-helix	62-66	5
α-helix	67-81	15
β-strand	91-97	7	10
α-helix	102-112	11
β-strand	143-147	5	10
α-helix	152-162	11
α-helix	163-165	3
β-strand	169-171	3	10
α-helix	177-180	4
β-strand	188-190	3	10
α-helix	196-208	13
β-strand	213-219	7	12
α-helix	222-236	15
β-strand	241-248	8	12
α-helix	254-265	12
β-strand	273-277	5	12
α-helix	280-292	13
β-strand	300-302	3	12
α-helix	318-321	4
β-strand	325-329	5	12
α-helix	332-334	3
α-helix	335-341	7
α-helix	355-362	8
β-strand	366	1	13
β-strand	380	1	13
α-helix	397-418	22
α-helix	427-429	3
α-helix	434-442	9
β-strand	445-447	3	14
β-strand	453-455	3	14
β-strand	466-475	10	12
β-strand	478-488	11	12
β-strand	491-492	2	12
α-helix	507-508	2
β-strand	520-523	4	15
β-strand	533-536	4	15
β-strand	541-543	3	16
β-strand	549-551	3	16
β-strand	556-558	3	17
α-helix	560-562	3
β-strand	565-567	3	17
α-helix	568-570	3
β-strand	571	1	18
α-helix	578-603	26
α-helix	617-635	19
α-helix	646-671	26
α-helix	690-692	3
α-helix	693-714	22
β-strand	719-722	4	18
β-strand	730-733	4	18
α-helix	738-761	24
α-helix	767-769	3
α-helix	770-777	8
α-helix	779-793	15
α-helix	798-826	29

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Metabotropic glutamate receptor 5	A, B	protein	836	Homo sapiens	P41594 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8X0G_1 Metabotropic glutamate receptor 5 (chains A, B)
QSSERRVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAMLHTLERIN
SDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRDSLISSEEEEGLVRCVDGSSSSFRSK
KPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQAR
AMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKL
LKKLTSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQRE
AVGGITIKLQSPDVKWFDDYYLKLRPETNLRNPWFQEFWQHRFQCRLEGFPQENSKYNKT
CNSSLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLCDAMKPIDGRKLLES
LMKTAFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDDEVW
SKKSNIIRSVCSEPCEKGQIKVIRKGEVSCCWTCTPCKENEYVFDEYTCKACQLGSWPTD
DLTGCDLIPVQYLRWGDPEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYI
ILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYSALVTKTNRIARILAGSKKKI
CTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTNLGV
VAPLGYNGLLILACTFYAFKTRNVPANFNEAKYIAFAMYTTCIIWLAFVPIYFGSNYKAI
TMCFSVSLSATVLLGCMFVPKVYIILAKPERNVRSAFTTSTVVRMHVGDGKSSSAA

Ligands and cofactors

ID	Name	Formula	Copies
QUS	(s)-2-amino-3-(3,5-dioxo-[1,2,4]OXADIAZOLIDIN-2-yl)-propionic acid	C5 H7 N3 O5	2
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	2

Primary citation

Conformational diversity in class C GPCR positive allosteric modulation. Cannone, G., Berto, L., Malhaire, F. et al. Nat Commun (2025) 16:619-619. DOI 10.1038/s41467-024-55439-9 · PubMed

Other PDB entries of the same protein (UniProt P41594 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6FFI 2.2 Å, Crystal Structure of mGluR5 in complex with MMPEP at 2.2 A
9HC0 2.33 Å, Dark structure of the human metabotropic glutamate receptor 5 transmembrane domain bound…
3LMK 2.44 Å, Ligand Binding Domain of Metabotropoc glutamate receptor mGluR5 complexed with glutamate
7P2L 2.54 Å, thermostabilised 7TM domain of human mGlu5 receptor bound to photoswitchable ligand…
4OO9 2.6 Å, Structure of the human class C GPCR metabotropic glutamate receptor 5 transmembrane…
5CGD 2.6 Å, Structure of the human class C GPCR metabotropic glutamate receptor 5 transmembrane…
6FFH 2.65 Å, Crystal Structure of mGluR5 in complex with Fenobam at 2.65 A
8TAO 2.9 Å, Quis and CDPPB bound active mGlu5
9HC3 2.9 Å, Apo-state structure of the human metabotropic glutamate receptor 5 transmembrane domain…
8T8M 3.0 Å, Quis-bound intermediate mGlu5
8X0B 3.1 Å, Human FL Metabotropic glutamate receptor 5, mGlu5-5M with Quisqualate and VU0424465
5CGC 3.1 Å, Structure of the human class C GPCR metabotropic glutamate receptor 5 transmembrane…

Browse structure collections

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