8X0B: Metabotropic glutamate receptor 5

Human FL Metabotropic glutamate receptor 5, mGlu5-5M with Quisqualate and VU0424465. Determined by electron microscopy at 3.1 Å resolution. Released 6 Nov 2024.

Method: Electron microscopy
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 2
Atoms: 12,415
Mol. weight: 195.38 kDa
Ligands: NAG, QUS, XQT
Released: 6 Nov 2024

Explore 8X0B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8X0B contains 59 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: 27 helices, 30 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	62-66	5
α-helix	67-81	15
β-strand	91-97	7	1
α-helix	102-112	11
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	196-208	13
β-strand	213-219	7	3
α-helix	223-238	16
β-strand	241-248	8	3
α-helix	254-265	12
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	434-441	8
β-strand	445-447	3	5
β-strand	453-455	3	5
β-strand	466-473	8	3
β-strand	479-488	10	3
β-strand	491-494	4	3
β-strand	520-523	4	6
β-strand	533-536	4	6
α-helix	537-538	2
β-strand	541-545	5	7
β-strand	548-551	4	7
β-strand	558	1	8
β-strand	565	1	8
β-strand	570-571	2	9
α-helix	578-601	24
α-helix	615-635	21
α-helix	641-674	34
α-helix	691-714	24
β-strand	719-720	2	10
β-strand	729-730	2	9
β-strand	732-733	2	10
α-helix	737-761	25
α-helix	770-787	18
α-helix	789-792	4
α-helix	798-816	19
α-helix	819-823	5

Chain B: 32 helices, 30 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
β-strand	60	1	12
α-helix	62-66	5
α-helix	67-81	15
β-strand	91-97	7	11
α-helix	102-113	12
β-strand	143-147	5	11
α-helix	152-162	11
α-helix	163-165	3
β-strand	169-171	3	11
α-helix	177-180	4
β-strand	188-190	3	11
α-helix	196-208	13
β-strand	213-219	7	13
α-helix	223-238	16
β-strand	241-248	8	13
α-helix	254-265	12
β-strand	273-277	5	13
α-helix	280-292	13
β-strand	300-302	3	13
α-helix	318-321	4
β-strand	325-329	5	13
α-helix	332-334	3
α-helix	335-341	7
α-helix	355-362	8
β-strand	366	1	14
β-strand	380	1	14
α-helix	381-382	2
α-helix	397-418	22
α-helix	427-429	3
α-helix	434-441	8
β-strand	445-447	3	15
β-strand	453-455	3	15
β-strand	466-472	7	13
β-strand	480-488	9	13
β-strand	491-494	4	13
α-helix	507-508	2
β-strand	523-524	2	16
β-strand	532-533	2	16
α-helix	536-538	3
β-strand	541-543	3	17
β-strand	549-551	3	17
β-strand	557-558	2	18
α-helix	560-562	3
β-strand	565-566	2	18
α-helix	568-569	2
β-strand	570	1	19
α-helix	578-603	26
α-helix	617-633	17
α-helix	641-678	38
α-helix	692-714	23
β-strand	719-720	2	20
β-strand	729	1	19
β-strand	732-733	2	20
α-helix	738-761	24
α-helix	770-787	18
α-helix	790-793	4
α-helix	800-814	15
α-helix	818-823	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Metabotropic glutamate receptor 5	A, B	protein	862	Homo sapiens	P41594 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8X0B_1 Metabotropic glutamate receptor 5 (chains A, B)
DYKDDDDKHHHHHHHHHHLEVLFQGPQSSERRVVAHMPGDIIIGALFSVHHQPTVDKVHE
RKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIR
DSLISSEEEEGLVRCVDGSSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSA
TSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDM
SAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSHLPKARVVACFCEGMTVRGLLMAMRRLG
LAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPETNLRNPW
FQEFWQHRFQCRLEGFPQENSKYNKTCNSSLTLKTHHVQDSKMGFVINAIYSMAYGLHNM
QMSLCPGYAGLCDAMKPIDGRKLLESLMKTAFTGVSGDTILFDENGDSPGRYEIMNFKEM
GKDYFDYINVGSWDNGELKMDDDEVWSKKSNIIRSVCSEPCEKGQIKVIRKGEVSCCWTC
TPCKENEYVFDEYTCKACQLGSWPTDDLTGCDLIPVQYLRWGDPEPIAAVVFACLGLLAT
LFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLS
PAMSYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIM
EPPDIMHDYPSIREVYLICNTTNLGVVAPLGYNGLLILACTFYAFKTRNVPANFNEAKYI
AFAMYTTCIIWLAFVPIYFGSNYKAITMCFSVSLSATVLLGCMFVPKVYIILAKPERNVR
SAFTTSTVVRMHVGDGKSSSAA

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	2
QUS	(s)-2-amino-3-(3,5-dioxo-[1,2,4]OXADIAZOLIDIN-2-yl)-propionic acid	C5 H7 N3 O5	2
XQT	VU0424465	C19 H19 F N2 O2	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…
5CGC 3.1 Å, Structure of the human class C GPCR metabotropic glutamate receptor 5 transmembrane…

Browse structure collections

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