P19493: Glutamate receptor 4 (Gria4)

Glutamate receptor 4 (Gria4) is a 902-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P19493.

Gene
Gria4
Organism
Rattus norvegicus
Length
902 residues
Mean pLDDT
82.8
Model
AF-P19493-F1 v6
Model created
1 Aug 2025
PDB structures
26

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.8 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate49%
70 to 90Confident: backbone generally right36%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions9%

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:12603841, PubMed:1372042, PubMed:19102704, PubMed:20107073, PubMed:2166337, PubMed:26966189). 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…

Subunit structure

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits (PubMed:19102704, PubMed:26966189). Tetramers may be formed by the dimerization of dimers (PubMed:26966189). Interacts with EPB41L1 via its C-terminus (PubMed:12574408). Isoform 3 interacts with PICK1 (PubMed:10027300). Found in a complex with GRIA1, GRIA2, GRIA3, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and…

Subcellular location

Cell membrane, Postsynaptic cell membrane, Cell projection, dendrite

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3FASX-ray1.4 ÅA/B=415-528, A/B=654-796
3EPEX-ray1.85 ÅA/B=416-528, A/B=654-795
3FATX-ray1.9 ÅA/B/C=415-528, A/B/C=654-796
3KEIX-ray1.9 ÅA/B=416-528, A/B=654-795
3KFMX-ray2.2 ÅA=416-528, A=654-795
4GPAX-ray2.25 ÅA=22-401
3EN3X-ray2.43 ÅA=416-528, A=654-795
5FWXX-ray2.5 ÅB/D=22-401
9QDNEM2.71 ÅA/B/C/D=21-902
9RMWEM2.9 ÅA/B/C/D=21-902
9RN7EM3.1 ÅA/B/C/D=21-902
9NR6EM3.26 ÅB/D=22-399
9P9BEM3.31 ÅA/B/C/D=25-848
9RN4EM3.4 ÅA/B/C/D=21-902
9IGZEM3.5 ÅA/B/C/D=21-902
9NR8EM3.53 ÅB/D=22-399
9QPWEM3.8 ÅA/B/C/D=21-902
9RMSEM3.8 ÅA/B/C/D=21-902
9P9DEM3.82 ÅA/B/C/D=25-848
9P9EEM3.82 ÅA/B/C/D=25-848

Showing 20 of 26 experimental structures (best resolution first).

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