Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator. Determined by X-ray diffraction at 1.4 Å resolution. Released 11 Jul 2012.
Explore 4FAT in 3D Show helices and sheets RCSB PDB PDBe
4FAT contains 15 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 |
|---|---|---|---|
| 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 | 153-164 | 12 | |
| β-strand | 171 | 1 | 7 |
| α-helix | 174-183 | 10 | |
| β-strand | 188-193 | 6 | 6 |
| α-helix | 194-201 | 8 | |
| β-strand | 208-211 | 4 | 6 |
| β-strand | 218-220 | 3 | 5 |
| β-strand | 223-225 | 3 | 1 |
| α-helix | 231-243 | 13 | |
| α-helix | 246-251 | 6 | |
| α-helix | 252-256 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate receptor 2 | A | protein | 263 | Rattus norvegicus | P19491 (AlphaFold model) |
>4FAT_1 Glutamate receptor 2 (chains A) GANKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGK YGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKGTP IESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVAR VRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLK LSEQGVLDKLKNKWWYDKGECGA
| ID | Name | Formula | Copies |
|---|---|---|---|
| 496 | 2-({[4-(hydroxymethyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]acetyl}amino)-4,5,6,… | C16 H17 F3 N4 O3 S | 1 |
| LI | Lithium ion | Li | 1 |
| GLU | Glutamic acid | C5 H9 N O4 | 1 |
Water and common crystallization additives (GOL, SO4) are not listed.
Functional analysis of a novel positive allosteric modulator of AMPA receptors derived from a structure-based drug design strategy. Harms, J.E., Benveniste, M., Maclean, J.K. et al. Neuropharmacology (2013) 64:45-52. DOI 10.1016/j.neuropharm.2012.06.008 · 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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