8FPG: GluA2 flip Q isoform of AMPA receptor
GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100uM CNQX (Closed-CaNaMg). Determined by electron microscopy at 2.32 Å resolution. Released 28 Feb 2024.
- Method
- Electron microscopy
- Resolution
- 2.32 Å
- Organisms
- Mus musculus, Rattus norvegicus
- Chains
- 8
- Atoms
- 10,674
- Mol. weight
- 546.82 kDa
- Released
- 28 Feb 2024
Explore 8FPG in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8FPG contains 56 α-helices and 28 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: 8 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 516-518 | 3 | |
| β-strand | 521 | 1 | 5 |
| α-helix | 523-545 | 23 | |
| α-helix | 548-550 | 3 | |
| α-helix | 573-584 | 12 | |
| α-helix | 596-628 | 33 | |
| β-strand | 787 | 1 | 6 |
| α-helix | 788 | 1 | |
| α-helix | 789-791 | 3 | |
| α-helix | 793-824 | 32 | |
Chain B: 10 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 509-513 | 5 | |
| α-helix | 516-518 | 3 | |
| β-strand | 521 | 1 | 4 |
| α-helix | 523-545 | 23 | |
| α-helix | 548-550 | 3 | |
| α-helix | 573-584 | 12 | |
| α-helix | 596-625 | 30 | |
| α-helix | 786 | 1 | |
| β-strand | 787 | 1 | 5 |
| α-helix | 788 | 1 | |
| α-helix | 789-791 | 3 | |
| α-helix | 793-824 | 32 | |
Chain C: 8 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 516-518 | 3 | |
| β-strand | 521 | 1 | 3 |
| α-helix | 523-545 | 23 | |
| α-helix | 548-550 | 3 | |
| α-helix | 573-585 | 13 | |
| α-helix | 596-628 | 33 | |
| β-strand | 787 | 1 | 4 |
| α-helix | 788 | 1 | |
| α-helix | 789-792 | 4 | |
| α-helix | 793-824 | 32 | |
Chain D: 10 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 509-513 | 5 | |
| α-helix | 516-518 | 3 | |
| β-strand | 521 | 1 | 6 |
| α-helix | 523-545 | 23 | |
| α-helix | 548-550 | 3 | |
| α-helix | 573-584 | 12 | |
| α-helix | 596-625 | 30 | |
| α-helix | 786 | 1 | |
| β-strand | 787 | 1 | 3 |
| α-helix | 788 | 1 | |
| α-helix | 789-792 | 4 | |
| α-helix | 793-824 | 32 | |
Chains E and G: 5 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-29 | 23 | |
| β-strand | 34-38 | 5 | 7 |
| β-strand | 57-61 | 5 | 7 |
| β-strand | 65-68 | 4 | 7 |
| β-strand | 77-79 | 3 | 7 |
| α-helix | 93-104 | 12 | |
| α-helix | 106-124 | 19 | |
| α-helix | 133-160 | 28 | |
| β-strand | 175 | 1 | 7 |
| α-helix | 178-213 | 36 | |
Chains F and H: 5 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-29 | 24 | |
| β-strand | 34-38 | 5 | 2 |
| β-strand | 57-61 | 5 | 2 |
| β-strand | 65-68 | 4 | 2 |
| β-strand | 77-79 | 3 | 2 |
| α-helix | 93-104 | 12 | |
| α-helix | 106-127 | 22 | |
| α-helix | 133-161 | 29 | |
| β-strand | 175-176 | 2 | 2 |
| α-helix | 178-213 | 36 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Voltage-dependent calcium channel gamma-2 subunit | E, F, G, H | protein | 336 | Mus musculus | O88602 (AlphaFold model) |
| Glutamate receptor 2 | A, B, C, D | protein | 889 | Rattus norvegicus | P19491 (AlphaFold model) |
Sequence of entity 1 (E, F, G, H), FASTA
>8FPG_1 Voltage-dependent calcium channel gamma-2 subunit (chains E, F, G, H)
MGLFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVCKTKSVSENETSEENEEVMTH
SGLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRASSIFPILSVILLFMGGL
CIAASEFYKTRHNIILSAGIFFVSAGLSNIIGIIVYISANAGDPSKSDSKKNSYSYGWSF
YFGALSFIIAEMVGVLAVHMFIDRHKQLRATARATDYLQASAITRIPSYRYRYQRRSRSS
SRSTEPSHSRDASPVGVKGFNTLPSTEISMYTLSRDPLKAATTPTATYNSDRDNSFLQVH
NCIQKDSKDSLHANTANRRTTPVGGRGGTETSQAPA
Sequence of entity 2 (A, B, C, D), FASTA
>8FPG_2 Glutamate receptor 2 (chains A, B, C, D)
MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTP
HIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDG
THPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINV
GNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANL
GFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALT
YDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNI
KFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTT
ILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKI
WNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLD
PLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWF
SLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDL
SKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGK
YAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLKLSEQGVL
DKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSR
AEAKRMKVAKNPQNINPSSSQNSQNFATDYKDDDDKEGYNVYGIESVKI
Primary citation
The open gate of the AMPA receptor forms a Ca 2+ binding site critical in regulating ion transport. Nakagawa, T., Wang, X.T., Miguez-Cabello, F.J. et al. Nat Struct Mol Biol (2024) 31:688-700. DOI 10.1038/s41594-024-01228-3 · PubMed
Other PDB entries of the same protein (UniProt O88602 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3JXT 1.5 Å, Crystal structure of the third PDZ domain of SAP-102 in complex with a fluorogenic…
- 8FQF 2.29 Å, GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2,…
- 8VHV 2.3 Å, Transmembrane AMPA Receptor Regulatory Protein Subunit Gamma 2
- 8FQ5 2.34 Å, GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma2, with…
- 8FQB 2.36 Å, GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma2, with…
- 8FPS 2.38 Å, GluA2 flip Q isoform N619K mutant of AMPA receptor in complex with gain-of-function TARP…
- 8FP4 2.4 Å, GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2,…
- 4X3H 2.4 Å, Crystal structure of arc N-lobe complexed with stargazin peptide
- 8FP9 2.44 Å, GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2,…
- 9B60 2.57 Å, GluA2 flip Q in complex with TARPgamma2 at pH8, consensus structure of TMD-TARPgamma2
- 9B5Z 2.71 Å, GluA2 flip Q in complex with TARPgamma2 at pH8, consensus structure of LBD-TMD-TARPgamma2
- 9B63 2.76 Å, GluA2 flip Q in complex with TARPgamma2 at pH5, consensus structure of TMD-TARPgamma2
Browse structure collections
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