P19490: Glutamate receptor 1 (Gria1)

Glutamate receptor 1 (Gria1) is a 907-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P19490.

Gene
Gria1
Organism
Rattus norvegicus
Length
907 residues
Mean pLDDT
80.9
Model
AF-P19490-F1 v6
Model created
1 Aug 2025
PDB structures
34

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.9 (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 accurate46%
70 to 90Confident: backbone generally right36%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions12%

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:2166337, PubMed:2168579). L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. 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 electrical impulse upon entry of monovalent and divalent cations such as sodium and calcium (PubMed:11773314, PubMed:18817736). The receptor then…

Subunit structure

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits; heteromeric assembly can be the result of both receptor subtype and flip-flop forms and according the composition, one partner can be dominant with respect to the fast desensitizing current component, whereas the other can determine the steady-state component (PubMed:1699275, PubMed:21639859, PubMed:2168579). Tetramers…

Subcellular location

Cell membrane, Endoplasmic reticulum membrane, Postsynaptic cell membrane, Postsynaptic density membrane, Cell projection, dendrite, Cell projection, dendritic spine, Early endosome membrane, Recycling endosome membrane, Presynapse, Synapse

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2AWWX-ray2.21 ÅC=890-907
2G2LX-ray2.35 ÅC/D=890-907
3SAJX-ray2.5 ÅA/B/C/D=22-392
8C2HEM2.64 ÅA/B/C/D=1-907
8C2IEM2.7 ÅA/B/C/D=1-907
8AYNEM2.8 ÅA/C=1-907
8C1QEM2.82 ÅA/B/C/D=1-907
8C1PEM2.9 ÅA/B/C/D=1-907
7OCEEM3.1 ÅA/C=1-907
8AYLEM3.2 ÅA/C=1-907
9OVUEM3.2 ÅA/C=1-841
9NR6EM3.26 ÅA/C=19-391
8AYMEM3.3 ÅA/C=1-907
8AYOEM3.3 ÅA/C=1-907
8P3TEM3.39 ÅA/B/C/D=1-907
7OCAEM3.4 ÅA/C=1-907
7OCCEM3.4 ÅA/C=1-907
9OVTEM3.43 ÅA/C=403-833
7OCDEM3.5 ÅA/C=1-907
7QHBEM3.5 ÅA/C=1-907

Showing 20 of 34 experimental structures (best resolution first).

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