9RMS: GluA4

GluA4 in complex with TARP-2, Resting II state, structure of TMD/LBD domains. Determined by electron microscopy at 3.8 Å resolution. Released 24 Sept 2025.

Method: Electron microscopy
Resolution: 3.8 Å
Organism: Rattus norvegicus
Chains: 8
Atoms: 18,061
Mol. weight: 539.84 kDa
Ligands: E2Q
Released: 24 Sept 2025

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

Secondary structure: helices and β-sheets

9RMS contains 96 α-helices and 106 β-strands across 8 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: 18 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	420-421	2	1
β-strand	429-430	2	2
α-helix	439-442	4
β-strand	443-444	2	2
α-helix	446-458	13
β-strand	465-466	2	1
β-strand	475	1	3
β-strand	482	1	3
α-helix	487-490	4
β-strand	497	1	1
β-strand	502	1	4
α-helix	505-508	4
β-strand	511	1	5
β-strand	518-520	3	4
β-strand	522	1	6
β-strand	524-527	4	7
β-strand	543	1	8
α-helix	545-567	23
α-helix	570-572	3
α-helix	597-607	11
α-helix	618-651	34
α-helix	653-655	3
α-helix	659-663	5
β-strand	668-670	3	7
β-strand	672	1	9
α-helix	676-683	8
α-helix	687-698	12
β-strand	705	1	9
α-helix	708-716	9
β-strand	722-724	3	7
β-strand	727	1	6
α-helix	728-735	8
β-strand	742-745	4	7
β-strand	752-754	3	4
β-strand	757	1	1
β-strand	759	1	5
α-helix	765-777	13
α-helix	780-785	6
α-helix	786-791	6
β-strand	809	1	10
α-helix	816-841	26

Chain B: 21 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	418-421	4	11
β-strand	429-430	2	12
α-helix	434-436	3
α-helix	439-442	4
β-strand	443-444	2	12
α-helix	446-458	13
β-strand	463-466	4	11
β-strand	475	1	13
β-strand	482	1	13
α-helix	484-490	7
β-strand	496-497	2	11
β-strand	502	1	14
α-helix	505-508	4
β-strand	511-513	3	11
α-helix	514	1
α-helix	516	1
β-strand	518-520	3	14
β-strand	522-527	6	15
β-strand	543	1	16
α-helix	545-568	24
α-helix	595-606	12
α-helix	618-651	34
α-helix	659-662	4
β-strand	668-670	3	15
β-strand	672	1	17
α-helix	676-683	8
α-helix	687-698	12
β-strand	705	1	17
α-helix	708-717	10
β-strand	722-727	6	15
α-helix	728-735	8
β-strand	742-745	4	15
β-strand	752-754	3	14
β-strand	757-759	3	11
α-helix	765-777	13
α-helix	780-786	7
α-helix	787-791	5
α-helix	808	1
β-strand	809	1	8
α-helix	810	1
α-helix	816-842	27

Chain C: 19 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	416	1
β-strand	417-421	5	18
β-strand	424	1	19
β-strand	428	1	19
β-strand	429-430	2	20
α-helix	434-436	3
α-helix	439-442	4
β-strand	443-444	2	20
α-helix	446-458	13
β-strand	462-466	5	18
β-strand	475	1	21
β-strand	482	1	21
α-helix	484-490	7
β-strand	496-497	2	18
β-strand	502	1	22
α-helix	505-508	4
β-strand	512-513	2	18
α-helix	514	1
α-helix	516	1
β-strand	518-520	3	22
β-strand	522-527	6	23
β-strand	543	1	24
α-helix	545-567	23
α-helix	595-607	13
α-helix	618-647	30
β-strand	668-670	3	23
β-strand	672	1	25
α-helix	676-683	8
α-helix	687-698	12
β-strand	705	1	25
α-helix	708-717	10
β-strand	722-727	6	23
α-helix	728-735	8
β-strand	742-745	4	23
β-strand	752-754	3	22
β-strand	757-758	2	18
α-helix	765-777	13
α-helix	780-786	7
α-helix	787-791	5
β-strand	809	1	16
α-helix	816-841	26

Chain D: 17 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	417-419	3	26
β-strand	429-430	2	27
α-helix	439-442	4
β-strand	443-444	2	27
α-helix	446-458	13
β-strand	462-464	3	26
β-strand	475-476	2	28
β-strand	481-482	2	28
α-helix	485-490	6
β-strand	496	1	26
β-strand	501-502	2	29
α-helix	503	1
α-helix	505-508	4
β-strand	511-513	3	30
β-strand	518-520	3	29
β-strand	522-527	6	31
β-strand	543	1	10
α-helix	545-568	24
α-helix	595-607	13
α-helix	618-645	28
α-helix	658-663	6
β-strand	668-670	3	31
β-strand	672	1	32
α-helix	676-682	7
α-helix	687-697	11
β-strand	705	1	32
α-helix	708-717	10
β-strand	722-727	6	31
α-helix	728-734	7
β-strand	742-745	4	31
β-strand	752-755	4	29
β-strand	757-759	3	30
α-helix	765-778	14
α-helix	780-786	7
α-helix	787-791	5
β-strand	809	1	24
α-helix	815-842	28

Chain E: 5 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	8-29	22
β-strand	34-38	5	33
β-strand	57-61	5	33
β-strand	65-68	4	33
β-strand	74	1	33
β-strand	77-79	3	33
α-helix	94-104	11
α-helix	106-124	19
α-helix	133-161	29
β-strand	176	1	33
α-helix	178-210	33

Chain F: 6 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	8-29	22
β-strand	34-38	5	34
β-strand	57-61	5	34
β-strand	65-68	4	34
β-strand	77-79	3	34
α-helix	80	1
α-helix	96-104	9
α-helix	106-127	22
α-helix	133-159	27
β-strand	175-176	2	34
α-helix	178-211	34

Chain G: 5 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	8-29	22
β-strand	34-38	5	35
β-strand	57-61	5	35
β-strand	65-68	4	35
β-strand	77-79	3	35
α-helix	94-104	11
α-helix	106-127	22
α-helix	133-159	27
β-strand	175-176	2	35
α-helix	178-211	34

Chain H: 5 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	8-29	22
β-strand	34-38	5	36
β-strand	57-61	5	36
β-strand	65-68	4	36
β-strand	77-79	3	36
α-helix	94-104	11
α-helix	106-122	17
α-helix	133-159	27
β-strand	175-176	2	36
α-helix	178-211	34

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Isoform 2 of Glutamate receptor 4	A, B, C, D	protein	882	Rattus norvegicus	P19493 (AlphaFold model)
Voltage-dependent calcium channel gamma-2 subunit	E, F, G, H	protein	323	Rattus norvegicus	Q71RJ2 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>9RMS_1 Isoform 2 of Glutamate receptor 4 (chains A, B, C, D)
GAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVT
NAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRG
ALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEE
LDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVT
GFQLVDFNTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKI
DISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELK
STGPRKVGYWNDMDKLVLIQDMPTLGNDTAAIENRTVVVTTIMESPYVMYKKNHEMFEGN
DKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAP
LTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSV
VLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSG
RIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEF
FRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPC
DTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEAGVLDKLKNKWWYDKGECGPKDS
GSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKLTFSEATRNKAR
LSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASDLP

Sequence of entity 2 (E, F, G, H), FASTA

>9RMS_2 Voltage-dependent calcium channel gamma-2 subunit (chains E, F, G, H)
MGLFDRGVQMLLTIVGAFAAFSLMTIAVGTDYWLYSRGVCKTKSVSENETSKKNEEVMTH
SGLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRASSIFPILSVILLFMGGL
CIAASEFYKTRHNIILSAGIFFVSAGLSNIIGIIVYISANAGDPSKSDSKKNSYSYGWSF
YFGALSFIIAEMVGVLAVHMFIDRHKQLRATARATDYLQASAITRIPSYRYRYQRRSRSS
SRSTEPSHSRDASPVGVKGFNTLPSTEISMYTLSRDPLKAATTPTATYNSDRDNSFLQVH
NCIQKDSKDSLHANTANRRTTPV

Ligands and cofactors

ID	Name	Formula	Copies
E2Q	6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide	C12 H8 N4 O6 S	4

Primary citation

GluA4 AMPA receptor gating mechanisms and modulation by auxiliary proteins. Vega-Gutierrez, C., Picanol-Parraga, J., Sanchez-Valls, I. et al. Nat Struct Mol Biol (2025) 32:2416-2428. DOI 10.1038/s41594-025-01666-7 · PubMed

Other PDB entries of the same protein (UniProt P19493 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3FAS 1.4 Å, X-ray structure of iGluR4 flip ligand-binding core (S1S2) in complex with (S)-glutamate…
3EPE 1.85 Å, Crystal Structure of the GluR4 Ligand-Binding domain in complex with glutamate
3FAT 1.9 Å, X-ray structure of iGluR4 flip ligand-binding core (S1S2) in complex with (S)-AMPA at…
3KEI 1.9 Å, Crystal Structure of the GluA4 Ligand-Binding domain L651V mutant in complex with…
3KFM 2.2 Å, Crystal Structure of the GluA4 Ligand-Binding domain L651V mutant in complex with kainate
4GPA 2.25 Å, High resolution structure of the GluA4 N-terminal domain (NTD)
3EN3 2.43 Å, Crystal Structure of the GluR4 Ligand-Binding domain in complex with kainate
5FWX 2.5 Å, Crystal structure of the AMPA receptor GluA2/A4 N-terminal domain heterodimer
9QDN 2.71 Å, GluA4 in complex with TARP-2, resting state I, structure of TMD/LBD
9RMW 2.9 Å, GluA4 in complex with TARP-2, open state, structure of TMD/LBD domains
9RN7 3.1 Å, GluA4 in complex with TARP-2, Desensitized state, structure of TMD domain
9NR6 3.26 Å, The structure of Noelin 1 with cerebellar GluA1/A4-ATD

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