P48169: Gamma-aminobutyric acid receptor subunit alpha-4 (GABRA4)

Gamma-aminobutyric acid receptor subunit alpha-4 (GABRA4) is a 554-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P48169.

Gene
GABRA4
Organism
Homo sapiens
Length
554 residues
Mean pLDDT
72.9
Model
AF-P48169-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 72.9 (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 accurate48%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions30%

What pLDDT means and how to read it

Function

Alpha subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:35355020). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha and beta subunit interface(s) (PubMed:35355020). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:35355020). GABAARs containing alpha-4 are predominantly extrasynaptic, contributing to tonic inhibition in dentate granule cells and…

Subunit structure

Heteropentamer, formed by a combination of alpha (GABRA1-6), beta (GABRB1-3), gamma (GABRG1-3), delta (GABRD), epsilon (GABRE), rho (GABRR1-3), pi (GABRP) and theta (GABRQ) chains, each subunit exhibiting distinct physiological and pharmacological properties

Subcellular location

Cell membrane, Postsynaptic cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7QN5EM2.5 ÅA=1-554
7QN9EM2.9 ÅA=1-554
7QNCEM2.9 ÅA=1-554
7QN7EM3.0 ÅA=1-554
7QNAEM3.0 ÅA=1-554

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