9WQO: GRM1-Acc State Conformation 1

GRM1-Acc State Conformation 1. Determined by electron microscopy at 2.9 Å resolution. Released 27 May 2026.

Method: Electron microscopy
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 12,256
Mol. weight: 196.78 kDa
Ligands: NAG, GGL
Released: 27 May 2026

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

Secondary structure: helices and β-sheets

9WQO contains 71 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 X: 34 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	35-37	3
β-strand	39-41	3	1
β-strand	45-51	7	1
β-strand	54	1	2
α-helix	55-58	4
α-helix	59-61	3
β-strand	70	1	2
α-helix	72-76	5
α-helix	77-91	15
β-strand	101-107	7	1
α-helix	112-123	12
α-helix	154-155	2
β-strand	156-160	5	1
α-helix	165-175	11
α-helix	176-178	3
β-strand	182-184	3	1
α-helix	190-193	4
β-strand	201-203	3	1
α-helix	208-221	14
β-strand	226-232	7	3
α-helix	235-251	17
β-strand	254-261	8	3
α-helix	267-279	13
β-strand	286-289	4	3
α-helix	293-305	13
β-strand	313-316	4	3
α-helix	324-327	4
α-helix	331-334	4
β-strand	338-342	5	3
α-helix	348-354	7
α-helix	368-376	9
β-strand	379	1	4
β-strand	393	1	4
α-helix	410-431	22
α-helix	440-442	3
α-helix	445-446	2
α-helix	447-455	9
β-strand	458-460	3	5
β-strand	466-468	3	5
β-strand	479-488	10	3
β-strand	491-501	11	3
β-strand	504-507	4	3
α-helix	526-528	3
β-strand	532-535	4	6
β-strand	546-549	4	6
β-strand	554-555	2	7
β-strand	563-564	2	7
α-helix	565-566	2
β-strand	569-571	3	8
β-strand	578-580	3	8
α-helix	581-583	3
β-strand	584	1	9
α-helix	591-616	26
α-helix	621-625	5
α-helix	628-649	22
α-helix	654-685	32
α-helix	704-727	24
β-strand	732-738	7	9
β-strand	741-746	6	9
α-helix	750-769	20
α-helix	773-776	4
α-helix	787-806	20
α-helix	811-840	30

Chain Y: 37 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	39-41	3	10
β-strand	45-51	7	10
β-strand	54	1	11
α-helix	55-58	4
α-helix	59-61	3
β-strand	70	1	11
α-helix	72-76	5
α-helix	77-91	15
β-strand	101-107	7	10
α-helix	112-123	12
α-helix	154-155	2
β-strand	156-160	5	10
α-helix	165-175	11
α-helix	176-178	3
β-strand	182-184	3	10
α-helix	190-193	4
β-strand	201-203	3	10
α-helix	208-221	14
β-strand	226-232	7	12
α-helix	235-250	16
β-strand	254-261	8	12
α-helix	267-278	12
β-strand	286-289	4	12
α-helix	293-306	14
β-strand	313-316	4	12
α-helix	324-327	4
α-helix	331-334	4
β-strand	338-342	5	12
α-helix	348-355	8
α-helix	368-376	9
β-strand	379	1	13
β-strand	393	1	13
α-helix	394	1
α-helix	410-431	22
α-helix	440-442	3
α-helix	445-446	2
α-helix	447-456	10
β-strand	458-460	3	14
β-strand	466-468	3	14
β-strand	479-486	8	12
β-strand	492-501	10	12
β-strand	504-507	4	12
α-helix	509-511	3
α-helix	526-528	3
β-strand	532-535	4	15
β-strand	546-549	4	15
α-helix	550-551	2
β-strand	554-558	5	16
β-strand	561-564	4	16
α-helix	565-566	2
β-strand	570-571	2	17
β-strand	578-579	2	17
β-strand	584	1	18
α-helix	591-616	26
α-helix	621-625	5
α-helix	628-648	21
α-helix	651-652	2
α-helix	654-685	32
α-helix	703-727	25
β-strand	732-738	7	18
β-strand	741-746	6	18
α-helix	750-769	20
α-helix	783-806	24
α-helix	811-835	25
α-helix	836-840	5
α-helix	842-844	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Metabotropic glutamate receptor 1	X, Y	protein	869	Homo sapiens	Q13255 (AlphaFold model)

Sequence of entity 1 (X, Y), FASTA

>9WQO_1 Metabotropic glutamate receptor 1 (chains X, Y)
DYKDDDDKTGASSQRSVARMDGDVIIGALFSVHHQPPAEKVPERKCGEIREQYGIQRVEA
MFHTLDKINADPVLLPNITLGSEIRDSCWHSSVALEQSIEFIRDSLISIRDEKDGINRCL
PDGQSLPPGRTKKPIAGVIGPGSSSVAIQVQNLLQLFDIPQIAYSATSIDLSDKTLYKYF
LRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEGNYGESGMDAFKELAAQEGLCIAHSDKI
YSNAGEKSFDRLLRKLRERLPKARVVVCFCEGMTVRGLLSAMRRLGVVGEFSLIGSDGWA
DRDEVIEGYEVEANGGITIKLQSPEVRSFDDYFLKLRLDTNTRNPWFPEFWQHRFQCRLP
GHLLENPNFKRICTGNESLEENYVQDSKMGFVINAIYAMAHGLQNMHHALCPGHVGLCDA
MKPIDGSKLLDFLIKSSFIGVSGEEVWFDEKGDAPGRYDIMNLQYTEANRYDYVHVGTWH
EGVLNIDDYKIQMNKSGVVRSVCSEPCLKGQIKVIRKGEVSCCWICTACKENEYVQDEFT
CKACDLGWWPNADLTGCEPIPVRYLEWSNIESIIAIAFSCLGILVTLFVTLIFVLYRDTP
VVKSSSRELCYIILAGIFLGYVCPFTLIAKPTTTSCYLQRLLVGLSSAMCYSALVTKTNR
IARILAGSKKKICTRKPRFMSAWAQVIIASILISVQLTLVVTLIIMEPPMPILSYPSIKE
VYLICNTSNLGVVAPLGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAF
VPIYFGSNYKIITTCFAVSLSVTVALGCMFTPKMYIIIAKPERNVRSAFTTSDVVRMHVG
DGKLPCRSNTFLNIFRRKKAGAGNANSNG

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	8
GGL	Gamma-L-glutamic acid	C5 H9 N O4	2

Water and common crystallization additives (CL) are not listed.

Primary citation

G protein selectivity in group I metabotropic glutamate receptors. Lu, Y., Wen, T., Lu, X. et al. Sci Adv (2026) 12:eaee0044-eaee0044. DOI 10.1126/sciadv.aee0044 · PubMed

Other PDB entries of the same protein (UniProt Q13255 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3KS9 1.9 Å, Metabotropic glutamate receptor mGluR1 complexed with LY341495 antagonist
4OR2 2.8 Å, Human class C G protein-coupled metabotropic glutamate receptor 1 in complex with a…
27TM 3.2 Å, GRM1-Acc State Conformation 2
9WQM 3.3 Å, GRM1-Gi Complex Structure
7DGE 3.65 Å, intermediate state of class C GPCR
9WQN 3.7 Å, GRM1-Gq Complex Structure
7DGD 3.96 Å, apo state of class C GPCR

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