GluA4, resting state, structure of TMD/LBD. Determined by electron microscopy at 3.8 Å resolution. Released 24 Sept 2025.
Explore 9QPW in 3D Show helices and sheets RCSB PDB PDBe
9QPW contains 72 α-helices and 72 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 417-421 | 5 | 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 | 462-466 | 5 | 1 |
| α-helix | 484-490 | 7 | |
| β-strand | 496 | 1 | 1 |
| β-strand | 497-500 | 4 | 3 |
| α-helix | 505-508 | 4 | |
| β-strand | 511-513 | 3 | 3 |
| α-helix | 514 | 1 | |
| β-strand | 522-527 | 6 | 4 |
| β-strand | 543 | 1 | 5 |
| α-helix | 545-564 | 20 | |
| α-helix | 598-607 | 10 | |
| α-helix | 618-651 | 34 | |
| α-helix | 658-663 | 6 | |
| β-strand | 668-670 | 3 | 4 |
| β-strand | 672 | 1 | 6 |
| α-helix | 676-682 | 7 | |
| α-helix | 687-698 | 12 | |
| β-strand | 705 | 1 | 6 |
| α-helix | 708-716 | 9 | |
| β-strand | 722-727 | 6 | 4 |
| α-helix | 728-735 | 8 | |
| β-strand | 742-745 | 4 | 4 |
| β-strand | 755-759 | 5 | 3 |
| α-helix | 766-778 | 13 | |
| α-helix | 780-786 | 7 | |
| α-helix | 787-791 | 5 | |
| β-strand | 809 | 1 | 7 |
| α-helix | 812-814 | 3 | |
| α-helix | 815-835 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 417-421 | 5 | 8 |
| β-strand | 429-430 | 2 | 9 |
| α-helix | 439-442 | 4 | |
| β-strand | 443-444 | 2 | 9 |
| α-helix | 446-458 | 13 | |
| β-strand | 462-466 | 5 | 8 |
| β-strand | 476 | 1 | 10 |
| β-strand | 481 | 1 | 10 |
| α-helix | 484-490 | 7 | |
| β-strand | 497-502 | 6 | 8 |
| α-helix | 503 | 1 | |
| α-helix | 505-510 | 6 | |
| β-strand | 511-513 | 3 | 8 |
| β-strand | 518 | 1 | 8 |
| β-strand | 521 | 1 | 11 |
| β-strand | 524-527 | 4 | 12 |
| α-helix | 530-535 | 6 | |
| α-helix | 538-540 | 3 | |
| β-strand | 543 | 1 | 13 |
| α-helix | 545-566 | 22 | |
| α-helix | 598-606 | 9 | |
| α-helix | 618-647 | 30 | |
| α-helix | 658-663 | 6 | |
| β-strand | 668-670 | 3 | 12 |
| β-strand | 672 | 1 | 14 |
| α-helix | 676-682 | 7 | |
| α-helix | 687-697 | 11 | |
| β-strand | 705 | 1 | 14 |
| α-helix | 708-717 | 10 | |
| β-strand | 722-724 | 3 | 12 |
| α-helix | 730-735 | 6 | |
| β-strand | 742-745 | 4 | 12 |
| β-strand | 751 | 1 | 11 |
| β-strand | 754-759 | 6 | 8 |
| α-helix | 765-778 | 14 | |
| α-helix | 780-790 | 11 | |
| β-strand | 809 | 1 | 5 |
| α-helix | 811-835 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Isoform 2 of Glutamate receptor 4 | A, B, C, D | protein | 882 | Rattus norvegicus | P19493 (AlphaFold model) |
>9QPW_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
| ID | Name | Formula | Copies |
|---|---|---|---|
| E2Q | 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide | C12 H8 N4 O6 S | 4 |
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:
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