8X0E: Metabotropic glutamate receptor 5

Human FL Metabotropic glutamate receptor 5, mGlu5-5M with agonist and PAM, W785A mutant. Determined by electron microscopy at 3.4 Å resolution. Released 6 Nov 2024.

Method: Electron microscopy
Resolution: 3.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 12,086
Mol. weight: 188.06 kDa
Ligands: QUS, NAG
Released: 6 Nov 2024

Explore 8X0E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8X0E contains 65 α-helices and 69 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, 32 β-strands

Element	Residues	Length	Sheet
β-strand	31	1	1
β-strand	35-41	7	2
β-strand	44	1	3
α-helix	45-48	4
β-strand	60	1	3
α-helix	62-67	6
α-helix	68-81	14
β-strand	91-92	2	2
β-strand	93	1	1
β-strand	95-97	3	2
α-helix	102-113	12
β-strand	143-148	6	2
α-helix	152-162	11
α-helix	163-165	3
β-strand	169-171	3	2
α-helix	177-180	4
β-strand	188-190	3	2
α-helix	195-208	14
β-strand	213-219	7	4
α-helix	222-238	17
β-strand	241-248	8	4
α-helix	254-265	12
β-strand	273-275	3	4
α-helix	280-293	14
β-strand	300-302	3	4
α-helix	311-313	3
α-helix	318-321	4
β-strand	325-329	5	4
α-helix	332-334	3
α-helix	335-342	8
α-helix	355-362	8
β-strand	366	1	5
β-strand	380	1	5
α-helix	397-418	22
α-helix	427-429	3
α-helix	434-441	8
β-strand	445-447	3	6
β-strand	453-455	3	6
β-strand	466-473	8	4
β-strand	479-483	5	4
β-strand	485-488	4	4
β-strand	491-494	4	4
α-helix	507-508	2
β-strand	521-523	3	7
β-strand	533-535	3	7
β-strand	541-543	3	8
β-strand	549-551	3	8
β-strand	557-558	2	9
α-helix	560-562	3
β-strand	565-566	2	9
α-helix	567-570	4
β-strand	571	1	10
α-helix	578-603	26
α-helix	615-635	21
α-helix	641-672	32
α-helix	692-714	23
β-strand	719-722	4	10
β-strand	730-733	4	10
α-helix	738-761	24
α-helix	770-793	24
α-helix	798-809	12
α-helix	819-823	5

Chain B: 35 helices, 37 β-strands

Element	Residues	Length	Sheet
β-strand	29-31	3	11
β-strand	35-41	7	11
β-strand	44	1	12
α-helix	45-48	4
α-helix	49-51	3
β-strand	60	1	12
α-helix	62-67	6
α-helix	68-75	8
β-strand	91-97	7	11
α-helix	102-113	12
α-helix	114-116	3
β-strand	143-147	5	11
α-helix	152-162	11
α-helix	163-165	3
β-strand	169-171	3	11
α-helix	178-180	3
β-strand	188-190	3	11
α-helix	196-208	13
β-strand	213-219	7	13
α-helix	223-235	13
β-strand	241-248	8	13
α-helix	254-265	12
β-strand	273-276	4	13
α-helix	280-293	14
β-strand	300-302	3	13
α-helix	318-321	4
β-strand	325	1	13
β-strand	328-329	2	14
α-helix	332-334	3
α-helix	336-342	7
α-helix	355-362	8
β-strand	366	1	15
β-strand	380	1	15
α-helix	393-394	2
α-helix	397-418	22
α-helix	427-429	3
α-helix	434-442	9
β-strand	445-447	3	16
β-strand	453-455	3	16
β-strand	466-467	2	14
β-strand	469-475	7	13
β-strand	478-483	6	13
β-strand	485	1	17
β-strand	487	1	14
β-strand	488	1	18
β-strand	491	1	18
β-strand	494	1	17
α-helix	507-508	2
β-strand	520	1	19
β-strand	523-524	2	20
β-strand	532-533	2	20
β-strand	536	1	19
β-strand	541-543	3	21
β-strand	549-551	3	21
β-strand	557-558	2	22
α-helix	560-562	3
β-strand	565-566	2	22
α-helix	567-570	4
β-strand	571	1	23
α-helix	578-603	26
α-helix	617-635	19
α-helix	641-672	32
α-helix	692-714	23
β-strand	720-722	3	23
β-strand	730-732	3	23
α-helix	737-761	25
α-helix	767-769	3
α-helix	770-787	18
α-helix	789-793	5
α-helix	798-809	12
α-helix	813-817	5
α-helix	819-824	6

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

>8X0E_1 Metabotropic glutamate receptor 5 (chains A, B)
QSSERRVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAMLHTLERIN
SDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRDSLISSEEEEGLVRCVDGSSSSFRSK
KPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQAR
AMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKL
LKKLTSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQRE
AVGGITIKLQSPDVKWFDDYYLKLRPETNLRNPWFQEFWQHRFQCRLEGFPQENSKYNKT
CNSSLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLCDAMKPIDGRKLLES
LMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDDEVW
SKKSNIIRSVCSEPCEKGQIKVIRKGEVSCCWTCTPCKENEYVFDEYTCKACQLGSWPTD
DLTGCDLIPVQYLRWGDPEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYI
ILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYSALVTKTNRIARILAGSKKKI
CTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTNLGV
VAPLGYNGLLILACTFYAFKTRNVPANFNEAKYIAFAMYTTCIIALAFVPIYFGSNYKAI
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
8X0G 3.0 Å, Human FL Metabotropic glutamate receptor 5, mGlu5-5M with quisqualate, Acc conformation…
8X0B 3.1 Å, Human FL Metabotropic glutamate receptor 5, mGlu5-5M with Quisqualate and VU0424465

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