9OVT: Glutamate receptor 1

Heteromeric GluA1/A2 in the inactive state, composite map of LBD-TMD. Determined by electron microscopy at 3.43 Å resolution. Released 8 Apr 2026.

Method: Electron microscopy
Resolution: 3.43 Å
Organism: Rattus norvegicus
Chains: 4
Atoms: 13,011
Mol. weight: 193.58 kDa
Ligands: ZK1
Released: 8 Apr 2026

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

Secondary structure: helices and β-sheets

9OVT contains 65 α-helices and 78 β-strands across 4 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: 17 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	391-395	5	1
β-strand	403-404	2	2
α-helix	408-410	3
α-helix	413-415	3
β-strand	417-418	2	2
α-helix	420-432	13
β-strand	436-440	5	1
β-strand	447	1	3
β-strand	458	1	3
α-helix	459-464	6
β-strand	470	1	1
β-strand	471	1	4
β-strand	474	1	5
α-helix	479-482	4
β-strand	485-486	2	6
β-strand	496-501	6	7
α-helix	519-542	24
α-helix	569-578	10
α-helix	592-624	33
β-strand	644	1	8
β-strand	646	1	9
α-helix	650-656	7
α-helix	661-670	10
β-strand	679	1	9
α-helix	682-691	10
β-strand	698	1	8
β-strand	699-701	3	7
α-helix	702-708	7
β-strand	716-719	4	7
β-strand	729	1	5
β-strand	731	1	4
β-strand	732-733	2	6
α-helix	740-751	12
α-helix	754-757	4
α-helix	759	1
α-helix	760-765	6
α-helix	790-814	25

Chains B and D: 15 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	394-399	6	10
β-strand	407-408	2	11
α-helix	409	1
β-strand	421-422	2	11
α-helix	424-436	13
β-strand	439-444	6	10
β-strand	453	1	12
β-strand	460	1	12
α-helix	465-468	4
β-strand	474	1	10
β-strand	475	1	13
β-strand	480	1	14
α-helix	483-486	4
β-strand	490	1	15
β-strand	500-505	6	16
α-helix	523-545	23
α-helix	573-584	12
α-helix	596-623	28
α-helix	637-641	5
β-strand	646-649	4	16
β-strand	650	1	17
α-helix	654-660	7
α-helix	665-676	12
β-strand	683	1	17
α-helix	686-695	10
β-strand	700-705	6	16
α-helix	706-712	7
β-strand	720-723	4	16
β-strand	732	1	14
β-strand	735	1	13
β-strand	736	1	15
α-helix	745-756	12
α-helix	758-767	10
α-helix	794-816	23

Chain C: 18 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	391-395	5	18
β-strand	403-404	2	19
α-helix	408-410	3
α-helix	413-415	3
β-strand	417-418	2	19
α-helix	420-432	13
β-strand	436-440	5	18
β-strand	447	1	20
β-strand	458	1	20
α-helix	459-464	6
β-strand	470	1	18
β-strand	471	1	21
β-strand	474	1	22
α-helix	479-482	4
β-strand	485-486	2	23
β-strand	496-501	6	24
α-helix	507-509	3
α-helix	519-542	24
α-helix	569-578	10
α-helix	592-624	33
β-strand	644	1	25
β-strand	646	1	26
α-helix	650-656	7
α-helix	661-670	10
β-strand	679	1	26
α-helix	682-691	10
β-strand	698	1	25
β-strand	699-701	3	24
α-helix	702-708	7
β-strand	716-719	4	24
β-strand	729	1	22
β-strand	731	1	21
β-strand	732-733	2	23
α-helix	740-751	12
α-helix	754-757	4
α-helix	759	1
α-helix	760-765	6
α-helix	790-814	25

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glutamate receptor 1	A, C	protein	431	Rattus norvegicus	P19490 (AlphaFold model)
Glutamate receptor 2	B, D	protein	429	Rattus norvegicus	P19491 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>9OVT_1 Glutamate receptor 1 (chains A, C)
SVQNRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDG
KYGARDPDTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQ
KSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEGRDQTTSDQS
NEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVER
MVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEE
GMIRVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRGPVNL
AVLKLSEQGVLDKLKSKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILIGGLGLAML
VALIEFCYKSR

Sequence of entity 2 (B, D), FASTA

>9OVT_2 Glutamate receptor 2 (chains B, D)
QKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYG
ARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSK
PGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEF
GIFNSLWFSLGAFMRQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVS
PIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVA
RVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVL
KLSEQGVLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVAL
IEFCYKSRA

Ligands and cofactors

ID	Name	Formula	Copies
ZK1	{[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl…	C14 H15 F3 N3 O6 P	4

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

Primary citation

Auxiliary subunits reshape structural asymmetry and functional plasticity in heterotetrameric GluA1/A2 AMPA receptor core. Yen, L.Y., Newton, T.P., Yelshanskaya, M.V. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-71063-1 · PubMed

Other PDB entries of the same protein (UniProt P19490 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2AWW 2.21 Å, Synapse associated protein 97 PDZ2 domain variant C378G with C-terminal GluR-A peptide
3SAJ 2.5 Å, Crystal Structure of glutamate receptor GluA1 Amino Terminal Domain
8C2H 2.64 Å, Transmembrane domain of active state homomeric GluA1 AMPA receptor in tandem with TARP…
8C2I 2.7 Å, Transmembrane domain of resting state homomeric GluA1 AMPA receptor in complex with TARP…
8AYN 2.8 Å, Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and ligand LY3130481
8C1Q 2.82 Å, Resting state homomeric GluA1 AMPA receptor in complex with TARP gamma 3
8C1P 2.9 Å, Active state homomeric GluA1 AMPA receptor in complex with TARP gamma 3
7OCE 3.1 Å, Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and CNIH2 (LBD-TMD)
8AYL 3.2 Å, Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and ligand JNJ-61432059
9OVU 3.2 Å, Composite map of GluA1/A2 in the activated state, in complex with positive allosteric…
9NR6 3.26 Å, The structure of Noelin 1 with cerebellar GluA1/A4-ATD
8AYM 3.3 Å, Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and ligand JNJ-55511118

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