9P9D: Active substate 2 of the GluA4 homotetramer

Active substate 2 of the GluA4 homotetramer. Determined by electron microscopy at 3.82 Å resolution. Released 28 Jan 2026.

Method: Electron microscopy
Resolution: 3.82 Å
Organisms: Rattus norvegicus, Mus musculus
Chains: 8
Atoms: 18,100
Mol. weight: 474.97 kDa
Ligands: CYZ, GLU
Released: 28 Jan 2026

Explore 9P9D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9P9D contains 115 α-helices and 103 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: 23 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	417-421	5	1
β-strand	429-430	2	2
β-strand	443-444	2	2
α-helix	446-458	13
β-strand	462-466	5	1
α-helix	467	1
α-helix	474	1
β-strand	475	1	3
α-helix	476	1
α-helix	481	1
β-strand	482	1	3
α-helix	483	1
α-helix	484-490	7
β-strand	496-497	2	1
β-strand	502	1	1
α-helix	505-508	4
β-strand	511-520	10	1
β-strand	522-527	6	4
α-helix	538-540	3
α-helix	545-548	4
α-helix	550-567	18
α-helix	595-606	12
α-helix	618-645	28
α-helix	658-663	6
β-strand	668-670	3	4
β-strand	672	1	5
α-helix	676-682	7
α-helix	687-696	10
β-strand	705	1	5
α-helix	708-717	10
β-strand	722-727	6	4
α-helix	728-736	9
β-strand	742-745	4	4
β-strand	752-759	8	1
α-helix	765-778	14
α-helix	780-786	7
α-helix	787-791	5
α-helix	811-813	3
α-helix	815-839	25

Chain B: 25 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	417-421	5	6
β-strand	424	1	7
β-strand	428	1	7
β-strand	429-430	2	8
α-helix	434-436	3
α-helix	439-442	4
β-strand	443-444	2	8
α-helix	446-458	13
β-strand	462-466	5	6
β-strand	475	1	9
β-strand	482	1	9
α-helix	484-490	7
β-strand	496	1	6
β-strand	497	1	10
α-helix	501	1
β-strand	502	1	11
α-helix	503	1
α-helix	505-508	4
β-strand	511-512	2	12
β-strand	518-520	3	11
β-strand	522-527	6	13
α-helix	529-531	3
β-strand	532	1	14
α-helix	533-535	3
α-helix	538-540	3
β-strand	543	1	15
α-helix	545-567	23
α-helix	595-606	12
α-helix	618-639	22
α-helix	642-647	6
β-strand	650	1	14
α-helix	658-662	5
β-strand	668	1	16
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	1	16
β-strand	724-727	4	13
α-helix	728-735	8
β-strand	742-745	4	13
β-strand	752-754	3	11
β-strand	757	1	10
β-strand	758-759	2	12
α-helix	765-778	14
α-helix	780-785	6
α-helix	786-790	5
α-helix	796	1
α-helix	811-813	3
α-helix	815-838	24

Chain C: 20 helices, 22 β-strands

Element	Residues	Length	Sheet
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	511-513	3	18
β-strand	518-520	3	22
β-strand	522-527	6	23
α-helix	528-531	4
α-helix	538-540	3
β-strand	543	1	24
α-helix	545-565	21
α-helix	595-606	12
α-helix	618-645	28
α-helix	660-663	4
β-strand	668-670	3	23
β-strand	672	1	25
α-helix	676-682	7
α-helix	687-698	12
β-strand	705	1	25
α-helix	708-718	11
β-strand	722-727	6	23
α-helix	728-736	9
β-strand	742-745	4	23
β-strand	752-754	3	22
β-strand	757-759	3	18
α-helix	765-777	13
α-helix	780-788	9
α-helix	790-792	3
β-strand	809	1	15
α-helix	811-813	3
α-helix	815-839	25

Chain D: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	417-421	5	26
β-strand	429-430	2	27
α-helix	434-436	3
α-helix	440-442	3
β-strand	443-444	2	27
α-helix	446-458	13
β-strand	462-466	5	26
β-strand	475	1	28
β-strand	482	1	28
α-helix	484-490	7
β-strand	496-497	2	26
β-strand	502	1	29
α-helix	505-508	4
β-strand	511-513	3	26
α-helix	514	1
α-helix	516	1
β-strand	518-520	3	29
β-strand	522-527	6	30
α-helix	528-534	7
α-helix	538-540	3
α-helix	545-567	23
α-helix	595-606	12
α-helix	618-639	22
α-helix	642-644	3
α-helix	658-662	5
β-strand	668-670	3	30
β-strand	672	1	31
α-helix	676-683	8
α-helix	687-698	12
β-strand	705	1	31
α-helix	708-717	10
β-strand	722-727	6	30
α-helix	728-736	9
β-strand	742-745	4	30
β-strand	752-754	3	29
β-strand	757-759	3	26
α-helix	765-778	14
α-helix	780-786	7
α-helix	787-791	5
α-helix	797-799	3
α-helix	808	1
β-strand	809	1	24
α-helix	810	1
α-helix	811-838	28

Chain E: 5 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	9-28	20
β-strand	34-38	5	35
β-strand	57-61	5	35
β-strand	65-68	4	35
β-strand	78-79	2	35
α-helix	96-104	9
α-helix	106-124	19
α-helix	133-159	27
β-strand	175-176	2	35
α-helix	178-209	32

Chain F: 6 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	9-29	21
β-strand	34-38	5	33
β-strand	57-61	5	33
β-strand	65-68	4	33
β-strand	77-79	3	33
α-helix	96-104	9
α-helix	106-124	19
α-helix	133-159	27
β-strand	175-176	2	33
α-helix	178-206	29
α-helix	207-209	3

Chain G: 5 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	8-28	21
β-strand	34-38	5	34
β-strand	57-61	5	34
β-strand	66-68	3	34
β-strand	77-78	2	34
α-helix	95-104	10
α-helix	106-126	21
α-helix	133-159	27
β-strand	175-176	2	34
α-helix	178-206	29

Chain H: 6 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	8-28	21
β-strand	34-36	3	32
β-strand	59-61	3	32
β-strand	65-68	4	32
β-strand	77-79	3	32
α-helix	80	1
α-helix	95-104	10
α-helix	106-124	19
α-helix	133-160	28
β-strand	175-176	2	32
α-helix	178-207	30

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Isoform 2 of Glutamate receptor 4	A, B, C, D	protein	846	Rattus norvegicus	P19493 (AlphaFold model)
Voltage-dependent calcium channel gamma-2 subunit	E, F, G, H	protein	209	Mus musculus	O88602 (AlphaFold model)

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

>9P9D_1 Isoform 2 of Glutamate receptor 4 (chains A, B, C, D)
MGKIMHISVLLSPVLWGLIFGVSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPF
NLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSF
PTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVS
AICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANL
GFKDISLERFIHGGANVTGFQLVDFNTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTY
DGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQ
FDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDMPTLGNDTAAIENRTVVVTTI
MESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIW
NGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDP
LAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFS
LGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLA
KQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKF
AFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEAGVLD
KLKNKWWYDKGECGPKDSGSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRA
EAKRMK

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

>9P9D_2 Voltage-dependent calcium channel gamma-2 subunit (chains E, F, G, H)
GLFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVCKTKSVSEDETSKKNEEVMTHS
GLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRASSIFPILSVILLFMGGLC
IAASEFYKTRHNIILSAGIFFVSAGLSNIIGIIVYISANAGDPSKSDSKKNSYSYGWSFY
FGALSFIIAEMVGVLAVHMFIDRHKQLTG

Ligands and cofactors

ID	Name	Formula	Copies
CYZ	Cyclothiazide	C14 H16 Cl N3 O4 S2	4
GLU	Glutamic acid	C5 H9 N O4	4

Primary citation

Structural basis for activation and conformational plasticity of the GluA4 AMPA receptor. Hale, W.D., Wang, H., Huganir, R.L. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-68953-9 · 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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