9RNH: GluA4
GluA4 in complex with TARP-2, Resting II state, structure of TMD domain. Determined by electron microscopy at 3.1 Å resolution. Released 24 Sept 2025.
- Method
- Electron microscopy
- Resolution
- 3.1 Å
- Organism
- Rattus norvegicus
- Chains
- 8
- Atoms
- 10,102
- Mol. weight
- 549.83 kDa
- Ligands
- PLM, OLC
- Released
- 24 Sept 2025
Explore 9RNH in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9RNH contains 39 α-helices and 31 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: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 543 | 1 | 1 |
| α-helix | 545-567 | 23 | |
| α-helix | 597-606 | 10 | |
| α-helix | 618-651 | 34 | |
| β-strand | 809 | 1 | 2 |
| α-helix | 816-906 | 26 | |
Chain B: 6 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 543 | 1 | 3 |
| α-helix | 545-568 | 24 | |
| α-helix | 595-606 | 12 | |
| α-helix | 618-650 | 33 | |
| α-helix | 808 | 1 | |
| β-strand | 809 | 1 | 1 |
| α-helix | 810 | 1 | |
| α-helix | 816-842 | 27 | |
Chain C: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 543 | 1 | 4 |
| α-helix | 545-567 | 23 | |
| α-helix | 595-607 | 13 | |
| α-helix | 618-647 | 30 | |
| β-strand | 809 | 1 | 3 |
| α-helix | 816-840 | 25 | |
Chain D: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 543 | 1 | 2 |
| α-helix | 545-568 | 24 | |
| α-helix | 595-606 | 12 | |
| α-helix | 618-645 | 28 | |
| β-strand | 809 | 1 | 4 |
| α-helix | 815-907 | 28 | |
Chain E: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-29 | 22 | |
| β-strand | 34-38 | 5 | 5 |
| β-strand | 57-61 | 5 | 5 |
| β-strand | 65-68 | 4 | 5 |
| β-strand | 74 | 1 | 5 |
| β-strand | 77-79 | 3 | 5 |
| α-helix | 94-104 | 11 | |
| α-helix | 106-124 | 19 | |
| α-helix | 133-161 | 29 | |
| β-strand | 176 | 1 | 5 |
| α-helix | 178-210 | 33 | |
Chain F: 6 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-29 | 22 | |
| β-strand | 34-38 | 5 | 6 |
| β-strand | 57-61 | 5 | 6 |
| β-strand | 65-68 | 4 | 6 |
| β-strand | 70 | 1 | 7 |
| β-strand | 74 | 1 | 7 |
| β-strand | 77-79 | 3 | 6 |
| α-helix | 80 | 1 | |
| α-helix | 96-104 | 9 | |
| α-helix | 106-127 | 22 | |
| α-helix | 133-160 | 28 | |
| β-strand | 175-176 | 2 | 6 |
| 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 | 8 |
| β-strand | 57-61 | 5 | 8 |
| β-strand | 65-68 | 4 | 8 |
| β-strand | 77-79 | 3 | 8 |
| α-helix | 94-104 | 11 | |
| α-helix | 106-127 | 22 | |
| α-helix | 133-159 | 27 | |
| β-strand | 175-176 | 2 | 8 |
| α-helix | 178-211 | 34 | |
Chain H: 5 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-29 | 22 | |
| β-strand | 34-37 | 4 | 9 |
| β-strand | 58-61 | 4 | 9 |
| β-strand | 65-68 | 4 | 9 |
| β-strand | 77-79 | 3 | 9 |
| α-helix | 94-104 | 11 | |
| α-helix | 106-122 | 17 | |
| α-helix | 133-159 | 27 | |
| β-strand | 175-176 | 2 | 9 |
| α-helix | 178-211 | 34 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Glutamate receptor | A, B, C, D | protein | 902 | Rattus norvegicus | A0A0G2JU28 (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
>9RNH_1 Glutamate receptor (chains A, B, C, D)
MRIICRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEA
PFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITP
SFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWH
VSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIA
NLGFKDISLERFIHGGANVTGFQLVDFNTPMVTKLMDRWKKLDQREYPGSETPPKYTSAL
TYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGN
VQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDMPTLGNDTAAIENRTVVVT
TIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTK
IWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFL
DPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLW
FSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAED
LAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKG
KFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEAGV
LDKLKNKWWYDKGECGPKDSGSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKS
RAEAKRMKLTFSEAIRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASD
LP
Sequence of entity 2 (E, F, G, H), FASTA
>9RNH_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 |
|---|
| PLM | Palmitic acid | C16 H32 O2 | 2 |
| OLC | (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate | C21 H40 O4 | 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
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