Complex NNNN of AMPA-subtype iGluR GluA2 in complex with auxiliary subunit gamma2 (Stargazin) at low glutamate concentration (20 uM) in the presence of cyclothiazide (100 uM). Determined by electron microscopy at 4.02 Å resolution. Released 20 Apr 2022.
Explore 7TNJ in 3D Show helices and sheets RCSB PDB PDBe
7TNJ contains 96 α-helices and 96 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 | 395-399 | 5 | 1 |
| β-strand | 407-408 | 2 | 2 |
| α-helix | 417-420 | 4 | |
| β-strand | 421-422 | 2 | 2 |
| α-helix | 424-436 | 13 | |
| β-strand | 440-444 | 5 | 1 |
| β-strand | 452-454 | 3 | 3 |
| β-strand | 459-461 | 3 | 3 |
| α-helix | 462-469 | 8 | |
| β-strand | 474 | 1 | 1 |
| β-strand | 475 | 1 | 4 |
| β-strand | 480 | 1 | 5 |
| α-helix | 483-488 | 6 | |
| β-strand | 489-491 | 3 | 4 |
| β-strand | 496-498 | 3 | 5 |
| β-strand | 500-505 | 6 | 6 |
| α-helix | 506-509 | 4 | |
| α-helix | 516-518 | 3 | |
| β-strand | 521 | 1 | 7 |
| α-helix | 523-544 | 22 | |
| α-helix | 573-584 | 12 | |
| α-helix | 596-629 | 34 | |
| α-helix | 636-641 | 6 | |
| β-strand | 646-648 | 3 | 6 |
| β-strand | 650 | 1 | 8 |
| α-helix | 654-660 | 7 | |
| α-helix | 665-676 | 12 | |
| β-strand | 683 | 1 | 8 |
| α-helix | 686-695 | 10 | |
| β-strand | 700-705 | 6 | 6 |
| α-helix | 706-712 | 7 | |
| β-strand | 720-723 | 4 | 6 |
| β-strand | 730-732 | 3 | 5 |
| β-strand | 735-737 | 3 | 4 |
| α-helix | 743-755 | 13 | |
| α-helix | 758-766 | 9 | |
| α-helix | 781-784 | 4 | |
| α-helix | 793-819 | 27 | |
| α-helix | 1007-1027 | 21 | |
| β-strand | 1033-1036 | 4 | 9 |
| β-strand | 1057-1060 | 4 | 9 |
| β-strand | 1064-1067 | 4 | 9 |
| β-strand | 1076-1078 | 3 | 9 |
| α-helix | 1094-1102 | 9 | |
| α-helix | 1106-1122 | 17 | |
| α-helix | 1133-1158 | 26 | |
| β-strand | 1174 | 1 | 9 |
| α-helix | 1178-1205 | 28 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 395-399 | 5 | 10 |
| β-strand | 407-408 | 2 | 11 |
| α-helix | 418-420 | 3 | |
| β-strand | 421-422 | 2 | 11 |
| α-helix | 424-436 | 13 | |
| β-strand | 440-444 | 5 | 10 |
| β-strand | 452-454 | 3 | 12 |
| β-strand | 459-461 | 3 | 12 |
| α-helix | 463-468 | 6 | |
| β-strand | 474 | 1 | 10 |
| β-strand | 475 | 1 | 13 |
| β-strand | 480 | 1 | 13 |
| α-helix | 483-488 | 6 | |
| β-strand | 490-498 | 9 | 13 |
| β-strand | 500-505 | 6 | 14 |
| α-helix | 506-507 | 2 | |
| α-helix | 516-518 | 3 | |
| α-helix | 523-546 | 24 | |
| α-helix | 573-584 | 12 | |
| α-helix | 596-623 | 28 | |
| α-helix | 628-632 | 5 | |
| α-helix | 638-641 | 4 | |
| β-strand | 646-648 | 3 | 14 |
| β-strand | 650 | 1 | 15 |
| α-helix | 654-660 | 7 | |
| α-helix | 665-675 | 11 | |
| β-strand | 683 | 1 | 15 |
| α-helix | 686-694 | 9 | |
| β-strand | 700-705 | 6 | 14 |
| α-helix | 706-714 | 9 | |
| β-strand | 720-723 | 4 | 14 |
| β-strand | 730-736 | 7 | 13 |
| α-helix | 743-755 | 13 | |
| α-helix | 758-769 | 12 | |
| α-helix | 775-778 | 4 | |
| β-strand | 787 | 1 | 7 |
| α-helix | 789-791 | 3 | |
| α-helix | 793-819 | 27 | |
| α-helix | 1005-1028 | 24 | |
| β-strand | 1033-1036 | 4 | 16 |
| β-strand | 1057-1060 | 4 | 16 |
| β-strand | 1066 | 1 | 17 |
| β-strand | 1076 | 1 | 17 |
| α-helix | 1093-1102 | 10 | |
| α-helix | 1105-1125 | 21 | |
| α-helix | 1133-1159 | 27 | |
| β-strand | 1174-1175 | 2 | 16 |
| α-helix | 1177-1208 | 32 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Isoform Flip of Glutamate receptor 2,Voltage-dependent calcium channel gamma-3 subunit chimera | A, B, C, D | protein | 1033 | Rattus norvegicus | P19491 (AlphaFold model), Q8VHX0 (AlphaFold model) |
>7TNJ_1 Isoform Flip of Glutamate receptor 2,Voltage-dependent calcium channel gamma-3 subunit chimera (chains A, B, C, D) NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRG VYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDETYRSLFQDLELKKE RRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRR GNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPR KIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLA AEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVI DFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPY EWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFT LIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDK MWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDS KGYGIATPKGSSLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSGSKEKTSALSL SNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKGTGLFDRGVQMLLTTVGAFAAFS LMTIAVGTDYWLYSRGVCKTKSVSEDETSKKNEEVMTHSGLWRTCCLEGNFKGLCKQIDH FPEDADYEADTAEYFLRAVRASSIFPILSVILLFMGGLCIAASEFYKTRHNIILSAGIFF VSAGLSNIIGIIVYISANAGDPSKSDSKKNSYSYGWSFYFGALSFIIAEMVGVLAVHMFI DRHKQLTGGLVPR
| ID | Name | Formula | Copies |
|---|---|---|---|
| CYZ | Cyclothiazide | C14 H16 Cl N3 O4 S2 | 4 |
Opening of glutamate receptor channel to subconductance levels. Yelshanskaya, M.V., Patel, D.S., Kottke, C.M. et al. Nature (2022) 605:172-178. DOI 10.1038/s41586-022-04637-w · PubMed
Other PDB entries of the same protein (UniProt P19491 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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