Gamma-aminobutyric acid receptor subunit alpha-1 (GABRA1) is a 456-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P14867.
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The mean pLDDT of this model is 81.7 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 65% |
| 70 to 90 | Confident: backbone generally right | 11% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
Alpha subunit of the heteropentameric ligand-gated chloride channel gated by Gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:23909897, PubMed:25489750, PubMed:29950725, PubMed:30602789). 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:29950725, PubMed:30602789). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:23909897, PubMed:29950725, PubMed:30602789). Alpha-1/GABRA1-containing…
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) subunits, each subunit exhibiting distinct physiological and pharmacological properties (PubMed:29950725, PubMed:30266951, PubMed:30602789). Interacts with UBQLN1 (By similarity). Interacts with TRAK1 (By similarity).…
Postsynaptic cell membrane, Cell membrane, Cytoplasmic vesicle membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9EQG | EM | 2.4 Å | A/D=28-456 |
| 9FAS | EM | 2.5 Å | A/D=37-445 |
| 9FFU | EM | 2.5 Å | A/D=32-339, A/D=418-456 |
| 6X3T | EM | 2.55 Å | B/D=28-339, B/D=419-456 |
| 8VRN | EM | 2.57 Å | B/D=28-339, B/D=418-456 |
| 8PET | EM | 2.6 Å | A/C=37-456 |
| 9FAJ | EM | 2.6 Å | A/D=37-449 |
| 9FAK | EM | 2.6 Å | A/D=37-449 |
| 9FGG | EM | 2.6 Å | A/D=28-456 |
| 8SGO | EM | 2.65 Å | B/D=28-339, B/D=418-456 |
| 7QNE | EM | 2.7 Å | A/D=1-456 |
| 9FG7 | EM | 2.7 Å | A/D=28-456 |
| 9FG9 | EM | 2.7 Å | A/D=28-456 |
| 8SID | EM | 2.71 Å | B/D=28-339, B/D=418-456 |
| 7PBZ | EM | 2.79 Å | A/D=32-339, A/D=418-456 |
| 9FAP | EM | 2.8 Å | A/D=39-443 |
| 9FFL | EM | 2.8 Å | A/D=32-339, A/D=418-456 |
| 9FFV | EM | 2.8 Å | A/D=32-339, A/D=418-456 |
| 8VQY | EM | 2.82 Å | B/D=28-339, B/D=418-456 |
| 6X40 | EM | 2.86 Å | B/D=28-339, B/D=418-456 |
Showing 20 of 86 experimental structures (best resolution first).
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