Crystal structure of the GluA2 LBD in complex with FW. Determined by X-ray diffraction at 1.23 Å resolution. Released 22 Feb 2017.
Explore 5JEI in 3D Show helices and sheets RCSB PDB PDBe
5JEI contains 16 α-helices and 20 β-strands across 1 chain. 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 |
|---|---|---|---|
| α-helix | 5 | 1 | |
| β-strand | 6-10 | 5 | 1 |
| β-strand | 13 | 1 | 2 |
| β-strand | 17 | 1 | 2 |
| β-strand | 18-19 | 2 | 3 |
| α-helix | 23-25 | 3 | |
| α-helix | 28-31 | 4 | |
| β-strand | 32-33 | 2 | 3 |
| α-helix | 35-47 | 13 | |
| β-strand | 51-55 | 5 | 1 |
| β-strand | 64 | 1 | 4 |
| β-strand | 71 | 1 | 4 |
| α-helix | 73-79 | 7 | |
| β-strand | 85-86 | 2 | 1 |
| β-strand | 91 | 1 | 5 |
| α-helix | 94-97 | 4 | |
| β-strand | 100-102 | 3 | 1 |
| α-helix | 103 | 1 | |
| α-helix | 105 | 1 | |
| β-strand | 107-109 | 3 | 5 |
| β-strand | 111-116 | 6 | 6 |
| α-helix | 124-128 | 5 | |
| β-strand | 134-136 | 3 | 6 |
| β-strand | 138 | 1 | 7 |
| α-helix | 142-149 | 8 | |
| α-helix | 153-162 | 10 | |
| β-strand | 171 | 1 | 7 |
| α-helix | 174-183 | 10 | |
| β-strand | 188-193 | 6 | 6 |
| α-helix | 194-200 | 7 | |
| β-strand | 208-211 | 4 | 6 |
| β-strand | 218-220 | 3 | 5 |
| β-strand | 223-225 | 3 | 1 |
| α-helix | 230-244 | 15 | |
| α-helix | 246-251 | 6 | |
| α-helix | 252-256 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate receptor 2,Glutamate receptor 2 | A | protein | 264 | Rattus norvegicus | P19491 (AlphaFold model) |
>5JEI_1 Glutamate receptor 2,Glutamate receptor 2 (chains A) GANKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGK YGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKGTP IESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIACFDKMWTYMRSAEPSVFVRTTAEGVAR VRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLK LNEQGLLDKLKNKWWYDKGECGSG
| ID | Name | Formula | Copies |
|---|---|---|---|
| FWD | 2-amino-3-(5-fluoro-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-propionic acid | C7 H8 F N3 O4 | 1 |
| PO4 | Phosphate ion | O4 P | 2 |
| TOE | 2-[2-(2-methoxy-ethoxy)-ethoxy]-ethoxyl | C7 H16 O4 | 1 |
| ETE | 2-{2-[2-2-(methoxy-ethoxy)-ethoxy]-ethoxy}-ethanol | C9 H20 O5 | 2 |
| PG0 | 2-(2-methoxyethoxy)ethanol | C5 H12 O3 | 1 |
Water and common crystallization additives (EDO, PEG, PG4, NA) are not listed.
Mechanism of partial agonism in AMPA-type glutamate receptors. Salazar, H., Eibl, C., Chebli, M. et al. Nat Commun (2017) 8:14327-14327. DOI 10.1038/ncomms14327 · 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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