Glutamate receptor 2 (Gria2) is a 883-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P19491.
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The mean pLDDT of this model is 84.8 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 62% |
| 70 to 90 | Confident: backbone generally right | 24% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid (PubMed:12015593, PubMed:12730367, PubMed:15591246, PubMed:2166337, PubMed:21846932, PubMed:9351977). L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system and plays an important role in fast excitatory synaptic transmission (By similarity). Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an…
Homotetramer or heterotetramer of pore-forming glutamate receptor subunits (PubMed:12015593, PubMed:12501192, PubMed:16483599, PubMed:19946266, PubMed:21317873). Tetramers may be formed by the dimerization of dimers (PubMed:12015593, PubMed:19946266, PubMed:21317873). May interact with MPP4 (By similarity). Forms a ternary complex with GRIP1 and CSPG4 (By similarity). Interacts with ATAD1 in an…
Cell membrane, Postsynaptic cell membrane, Postsynaptic density membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6YK4 | X-ray | 1.0 Å | A=413-527, A=653-797 |
| 5NG9 | X-ray | 1.15 Å | A=413-527, A=653-797 |
| 6YK5 | X-ray | 1.15 Å | A=413-527, A=653-797 |
| 6YK3 | X-ray | 1.2 Å | A=413-527, A=653-797 |
| 5JEI | X-ray | 1.23 Å | A=413-527, A=653-797 |
| 4IGT | X-ray | 1.24 Å | A=413-527, A=653-796 |
| 4YU0 | X-ray | 1.26 Å | A/B=413-527, A/B=653-796 |
| 5NIH | X-ray | 1.3 Å | A/B=413-527, A/B=653-797 |
| 1MQI | X-ray | 1.35 Å | A=413-527, A=653-796 |
| 5FTI | X-ray | 1.35 Å | A/B=404-527, A/B=653-796 |
| 4U21 | X-ray | 1.39 Å | A/B=413-527, A/B=634-796 |
| 4FAT | X-ray | 1.4 Å | A=413-796 |
| 6FAZ | X-ray | 1.4 Å | A/B=413-527, A/B=653-797 |
| 6Q54 | X-ray | 1.4 Å | A/B=413-527, A/B=653-797 |
| 4U2R | X-ray | 1.41 Å | A/B/C/D=413-527, A/B/C/D=653-796 |
| 4U22 | X-ray | 1.44 Å | A=413-527, A=653-796 |
| 5NS9 | X-ray | 1.44 Å | A/B=413-527, A/B=653-797 |
| 3TKD | X-ray | 1.45 Å | A/B=413-527, A/B=653-796 |
| 4Z0I | X-ray | 1.45 Å | A/B=413-527, A/B=653-796 |
| 1M5E | X-ray | 1.46 Å | A/B/C=413-527, A/B/C=653-796 |
Showing 20 of 337 experimental structures (best resolution first).
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