Gamma-aminobutyric acid receptor subunit beta-3 (GABRB3) is a 473-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P28472.
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The mean pLDDT of this model is 80.1 (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 | 62% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 20% |
What pLDDT means and how to read it
Beta subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:14993607, PubMed:18514161, PubMed:22243422, PubMed:22303015, PubMed:24909990, PubMed:26950270, 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:24909990, PubMed:30140029, PubMed:30602789). GABAARs containing beta-3/GABRB3 subunit are found at both synaptic and extrasynaptic sites (By similarity). When activated by GABA, GABAARs…
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 (PubMed:14993607, PubMed:18281286, PubMed:18514161, PubMed:22243422, PubMed:22303015, PubMed:24909990, PubMed:30140029, PubMed:30602789,…
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 |
|---|---|---|---|
| 7A5V | EM | 1.7 Å | A=26-303, A=305-332, A=447-473 |
| 9EQG | EM | 2.4 Å | B/E=1-473 |
| 6QFA | EM | 2.49 Å | A/B/C/D/E=26-332, A/B/C/D/E=447-473 |
| 7QN5 | EM | 2.5 Å | B/C/D=1-473 |
| 9FAS | EM | 2.5 Å | B/E=32-472 |
| 9FEU | EM | 2.5 Å | A/B/C/D/E=26-332, A/B/C/D/E=447-473 |
| 9FFU | EM | 2.5 Å | B/C/E=26-332, B/C/E=447-473 |
| 9G2E | EM | 2.5 Å | A/B/C/D/E=26-332 |
| 8PET | EM | 2.6 Å | B/D/E=26-473 |
| 9FAJ | EM | 2.6 Å | B/E=32-472 |
| 9FAK | EM | 2.6 Å | B/E=32-472 |
| 9FEX | EM | 2.6 Å | A/B/C/D/E=26-332, A/B/C/D/E=447-473 |
| 9FGG | EM | 2.6 Å | B/E=26-473 |
| 7QNE | EM | 2.7 Å | B/E=1-473 |
| 9FG7 | EM | 2.7 Å | B/E=26-473 |
| 9FG9 | EM | 2.7 Å | B/E=26-473 |
| 9G2D | EM | 2.7 Å | A/B/C/D/E=26-332 |
| 7PBZ | EM | 2.79 Å | B/C/E=26-332, B/C/E=447-473 |
| 9FAP | EM | 2.8 Å | B/E=34-472 |
| 9FF2 | EM | 2.8 Å | A/B/C/D/E=26-332, A/B/C/D/E=447-473 |
Showing 20 of 95 experimental structures (best resolution first).
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