P19492: Glutamate receptor 3 (Gria3)

Glutamate receptor 3 (Gria3) is a 888-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P19492.

Gene
Gria3
Organism
Rattus norvegicus
Length
888 residues
Mean pLDDT
83.9
Model
AF-P19492-F1 v6
Model created
1 Aug 2025
PDB structures
33

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Model confidence (pLDDT)

The mean pLDDT of this model is 83.9 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate53%
70 to 90Confident: backbone generally right32%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

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:1699567, PubMed:1709304, PubMed:2166337, PubMed:2168579). 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 inducing long-term potentiation (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…

Subunit structure

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits (PubMed:21317871). Tetramers may be formed by the dimerization of dimers (PubMed:21317871). Interacts with PICK1, GRIP1 and GRIP2 (PubMed:10027300, PubMed:10414981, PubMed:9069286). Found in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 (PubMed:19265014). Interacts…

Subcellular location

Cell membrane, Postsynaptic cell membrane, Postsynaptic density membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3LSWX-ray1.75 ÅA=417-530
4F29X-ray1.75 ÅA=417-530, A=658-799
3M3KX-ray1.79 ÅA/C/E=417-530, A/C/E=658-799
4F1YX-ray1.79 ÅA/C=417-530, A/C=658-799
4F3BX-ray1.82 ÅA=417-530, A=658-799
4F39X-ray1.83 ÅA=417-530, A=658-799
3DLNX-ray1.91 ÅA=416-530, A=658-799
4F2OX-ray1.91 ÅA=417-530, A=658-799
6FPJX-ray1.96 ÅA/B/C=23-403
3LSXX-ray2.01 ÅA=417-530, A=658-769
4F22X-ray2.06 ÅA=417-530, A=658-799
4F3GX-ray2.06 ÅA=417-530, A=658-799
3DP4X-ray2.11 ÅA=416-530, A=658-799
5FWYX-ray2.12 ÅB/D=23-403
3O21X-ray2.2 ÅA/B/C/D=23-403
4F2QX-ray2.2 ÅA=417-530, A=658-799
4F31X-ray2.29 ÅB/D=417-530, B/D=658-799
3RT8X-ray2.43 ÅA=417-530, A=658-799
3M3FX-ray2.5 ÅA=417-530, A=658-799
6FLRX-ray2.51 ÅA/B=23-403

Showing 20 of 33 experimental structures (best resolution first).

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