O14764: Gamma-aminobutyric acid receptor subunit delta (GABRD)

Gamma-aminobutyric acid receptor subunit delta (GABRD) is a 452-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O14764.

Gene
GABRD
Organism
Homo sapiens
Length
452 residues
Mean pLDDT
79.2
Model
AF-O14764-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.2 (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 right29%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions18%

What pLDDT means and how to read it

Function

Delta 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 delta/GABRD subunits are predominantly located in extrasynaptic or perisynaptic positions on hippocampus 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

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7QN5EM2.5 ÅE=1-452
7QN6EM2.9 ÅE=1-452
7QN9EM2.9 ÅE=1-452
7QNCEM2.9 ÅE=1-452
7QN7EM3.0 ÅE=1-452
7QN8EM3.1 ÅE=1-452
7QNDEM3.4 ÅE=1-452

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