8C1S: Glutamate receptor 2
Transmembrane domain of resting state homomeric GluA2 F231A mutant AMPA receptor in complex with TARP gamma 2. Determined by electron microscopy at 3.0 Å resolution. Released 30 Aug 2023.
- Method
- Electron microscopy
- Resolution
- 3.0 Å
- Organism
- Rattus norvegicus
- Chains
- 8
- Atoms
- 10,668
- Mol. weight
- 549.16 kDa
- Ligands
- POV, OLC, PLM
- Released
- 30 Aug 2023
Explore 8C1S in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8C1S contains 53 α-helices and 32 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 | 510-513 | 4 | |
| α-helix | 516-518 | 3 | |
| β-strand | 521 | 1 | 1 |
| α-helix | 523-544 | 22 | |
| α-helix | 573-584 | 12 | |
| α-helix | 596-628 | 33 | |
| β-strand | 787 | 1 | 2 |
| α-helix | 788 | 1 | |
| α-helix | 789-791 | 3 | |
| α-helix | 793-819 | 27 | |
Chain B: 9 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 510-513 | 4 | |
| α-helix | 516-518 | 3 | |
| β-strand | 521 | 1 | 3 |
| α-helix | 523-545 | 23 | |
| α-helix | 548-550 | 3 | |
| α-helix | 574-584 | 11 | |
| α-helix | 596-625 | 30 | |
| α-helix | 785-786 | 2 | |
| β-strand | 787 | 1 | 1 |
| α-helix | 788 | 1 | |
| α-helix | 793-822 | 30 | |
Chain C: 7 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 | 573-584 | 12 | |
| α-helix | 596-628 | 33 | |
| β-strand | 787 | 1 | 3 |
| α-helix | 788 | 1 | |
| α-helix | 793-820 | 28 | |
Chain D: 9 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 508-513 | 6 | |
| α-helix | 516-518 | 3 | |
| β-strand | 521 | 1 | 2 |
| α-helix | 523-544 | 22 | |
| α-helix | 573-584 | 12 | |
| α-helix | 596-625 | 30 | |
| α-helix | 786 | 1 | |
| β-strand | 787 | 1 | 4 |
| α-helix | 788 | 1 | |
| α-helix | 789-791 | 3 | |
| α-helix | 793-822 | 30 | |
Chain E: 5 helices, 4 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 | 67-68 | 2 | 5 |
| α-helix | 93-103 | 11 | |
| α-helix | 106-124 | 19 | |
| α-helix | 134-159 | 26 | |
| β-strand | 176 | 1 | 5 |
| α-helix | 178-209 | 32 | |
Chain F: 5 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-27 | 22 | |
| β-strand | 34 | 1 | 6 |
| β-strand | 37-38 | 2 | 7 |
| β-strand | 57-58 | 2 | 7 |
| β-strand | 59 | 1 | 8 |
| β-strand | 65-67 | 3 | 9 |
| β-strand | 68 | 1 | 8 |
| β-strand | 77-79 | 3 | 9 |
| α-helix | 93-103 | 11 | |
| α-helix | 106-126 | 21 | |
| α-helix | 134-159 | 26 | |
| β-strand | 176 | 1 | 6 |
| α-helix | 178-207 | 30 | |
Chain G: 5 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-29 | 22 | |
| β-strand | 34-38 | 5 | 10 |
| β-strand | 57-61 | 5 | 10 |
| β-strand | 65-68 | 4 | 10 |
| β-strand | 77-79 | 3 | 10 |
| α-helix | 93-103 | 11 | |
| α-helix | 106-126 | 21 | |
| α-helix | 133-161 | 29 | |
| β-strand | 174-176 | 3 | 10 |
| α-helix | 178-207 | 30 | |
Chain H: 5 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-29 | 24 | |
| β-strand | 34 | 1 | 11 |
| β-strand | 36-38 | 3 | 12 |
| β-strand | 57-59 | 3 | 12 |
| β-strand | 65-67 | 3 | 13 |
| β-strand | 68 | 1 | 12 |
| β-strand | 77-79 | 3 | 13 |
| α-helix | 94-103 | 10 | |
| α-helix | 106-123 | 18 | |
| α-helix | 134-160 | 27 | |
| β-strand | 176 | 1 | 11 |
| α-helix | 178-208 | 31 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Glutamate receptor 2 | A, B, C, D | protein | 891 | Rattus norvegicus | P19491 (AlphaFold model) |
| Voltage-dependent calcium channel gamma-2 subunit | E, F, G, H | protein | 322 | Rattus norvegicus | Q71RJ2 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>8C1S_1 Glutamate receptor 2 (chains A, B, C, D)
MQKIMHISVLLSPVLWGLIFGDYKDDDDKVSSNSIQIGGLFPRGADQEYSAFRVGMVQFS
TSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFI
TPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKK
WQVTAINVGNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKG
YHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTAT
IKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQ
VEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLE
NKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYG
ARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSK
PGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEF
GIFNSLWFSLGAFMRQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVS
PIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVA
RVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLRTPVNLAVL
KLSEQGVLDKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAMLVAL
IEFCYKSRAEAKRMKVAKNPQNINPSSSQNSQNFATYKEGYNVYGIESVKI
Sequence of entity 2 (E, F, G, H), FASTA
>8C1S_2 Voltage-dependent calcium channel gamma-2 subunit (chains E, F, G, H)
GLFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVCKTKSVSENETSKKNEEVMTHS
GLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRASSIFPILSVILLFMGGLC
IAASEFYKTRHNIILSAGIFFVSAGLSNIIGIIVYISANAGDPSKSDSKKNSYSYGWSFY
FGALSFIIAEMVGVLAVHMFIDRHKQLRATARATDYLQASAITRIPSYRYRYQRRSRSSS
RSTEPSHSRDASPVGVKGFNTLPSTEISMYTLSRDPLKAATTPTATYNSDRDNSFLQVHN
CIQKDSKDSLHANTANRRTTPV
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| POV | (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl… | C42 H82 N O8 P | 4 |
| OLC | (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate | C21 H40 O4 | 4 |
| PLM | Palmitic acid | C16 H32 O2 | 6 |
Primary citation
Structural mobility tunes signalling of the GluA1 AMPA glutamate receptor. Zhang, D., Ivica, J., Krieger, J.M. et al. Nature (2023) 621:877-882. DOI 10.1038/s41586-023-06528-0 · PubMed
Other PDB entries of the same protein (UniProt P19491 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6YK4 1.0 Å, Structure of the AMPA receptor GluA2o ligand-binding domain (S1S2J) in complex with the…
- 5NG9 1.15 Å, Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with agonist…
- 6YK5 1.15 Å, Structure of the AMPA receptor GluA2o ligand-binding domain (S1S2J) in complex with the…
- 6YK3 1.2 Å, Structure of the AMPA receptor GluA2o ligand-binding domain (S1S2J) in complex with the…
- 5JEI 1.23 Å, Crystal structure of the GluA2 LBD in complex with FW
- 4IGT 1.24 Å, Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the agonist…
- 4YU0 1.26 Å, Crystal structure of a tetramer of GluA2 TR mutant ligand binding domains bound with…
- 5NIH 1.3 Å, Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with agonist…
- 1MQI 1.35 Å, Crystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with…
- 5FTI 1.35 Å, Crystal structure of the GluA2 K738M-T744K LBD in complex with glutamate (lithium form)
- 4U21 1.39 Å, GluA2flip sLBD complexed with FW and (R,R)-2b crystal form E
- 4FAT 1.4 Å, Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an…
Browse structure collections
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