9IGZ: GluA4

GluA4 in complex with TARP-2, resting state, structure of N-terminal domain. Determined by electron microscopy at 3.5 Å resolution. Released 24 Sept 2025.

Method: Electron microscopy
Resolution: 3.5 Å
Organism: Rattus norvegicus
Chains: 4
Atoms: 11,676
Mol. weight: 394.69 kDa
Released: 24 Sept 2025

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

Secondary structure: helices and β-sheets

9IGZ contains 55 α-helices and 74 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: 14 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	26-33	8	14
α-helix	38-52	15
β-strand	63-70	8	14
α-helix	76-89	14
β-strand	93-96	4	14
α-helix	103-113	11
β-strand	116-119	4	14
α-helix	122-124	3
β-strand	131-133	3	14
α-helix	138-149	12
β-strand	153-158	6	15
α-helix	166-177	12
β-strand	180-185	6	15
α-helix	191-204	14
β-strand	208-212	5	15
α-helix	215-228	14
β-strand	236-239	4	15
β-strand	243	1	15
α-helix	244-246	3
α-helix	250-254	5
β-strand	259-263	5	15
α-helix	270-279	10
α-helix	293-295	3
α-helix	296-317	22
α-helix	340-350	11
β-strand	353-356	4	16
β-strand	359-363	5	16
β-strand	369-370	2	16
β-strand	373-380	8	15
β-strand	383-391	9	15
β-strand	395-398	4	15

Chains B and D: 13 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	26-33	8	9
α-helix	38-52	15
β-strand	63-70	8	9
α-helix	76-88	13
β-strand	93-95	3	9
α-helix	103-112	10
β-strand	116-119	4	9
β-strand	131-133	3	9
α-helix	136-137	2
α-helix	139-149	11
β-strand	155-158	4	10
α-helix	165-177	13
β-strand	182-185	4	10
α-helix	191-203	13
β-strand	208-212	5	10
α-helix	215-228	14
β-strand	232	1	11
β-strand	236-239	4	10
β-strand	243	1	10
α-helix	244-246	3
α-helix	250-255	6
β-strand	256	1	11
β-strand	258-263	6	10
α-helix	270-280	11
α-helix	296-317	22
α-helix	342-350	9
β-strand	353-356	4	12
β-strand	359-362	4	12
β-strand	363	1	13
β-strand	369	1	13
β-strand	373-379	7	10
β-strand	384-391	8	10
β-strand	395-398	4	10

Chain C: 15 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	26-33	8	6
α-helix	38-52	15
α-helix	62	1
β-strand	63-70	8	6
α-helix	76-89	14
β-strand	93-96	4	6
α-helix	103-113	11
β-strand	116-119	4	6
α-helix	122-124	3
β-strand	131-133	3	6
α-helix	138-149	12
β-strand	153-158	6	7
α-helix	166-177	12
β-strand	180-185	6	7
α-helix	191-204	14
β-strand	208-212	5	7
α-helix	215-228	14
β-strand	236-239	4	7
β-strand	243	1	7
α-helix	244-246	3
α-helix	250-254	5
β-strand	259-263	5	7
α-helix	270-279	10
α-helix	293-295	3
α-helix	296-317	22
α-helix	340-350	11
β-strand	353-356	4	8
β-strand	359-363	5	8
β-strand	369-370	2	8
β-strand	373-380	8	7
β-strand	383-391	9	7
β-strand	395-398	4	7

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)

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

>9IGZ_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

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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