Gamma-aminobutyric acid receptor subunit beta-2 (GABRB2) is a 512-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P47870.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 76.5 (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 | 55% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 25% |
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:19763268, PubMed:27789573, PubMed:29950725, PubMed:8264558). 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). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (By similarity). Chloride influx into the postsynaptic neuron following GABAAR opening decreases…
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:29950725, PubMed:8264558). Interacts with UBQLN1 (By similarity). May interact with KIF21B (By similarity). Identified in a complex…
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 |
|---|---|---|---|
| 6X3T | EM | 2.55 Å | A/C=25-331, A/C=487-512 |
| 8VRN | EM | 2.57 Å | A/C=25-331 |
| 8SGO | EM | 2.65 Å | A/C=25-331, A/C=486-512 |
| 8SID | EM | 2.71 Å | A/C=25-331, A/C=486-512 |
| 8VQY | EM | 2.82 Å | A/C=25-331 |
| 6X40 | EM | 2.86 Å | A/C=25-331, A/C=487-512 |
| 8DD2 | EM | 2.9 Å | A/C=25-331, A/C=486-511 |
| 8DD3 | EM | 2.9 Å | A/C=25-331, A/C=486-511 |
| 9CRS | EM | 2.9 Å | A/C=25-512 |
| 6X3X | EM | 2.92 Å | A/C=25-331, A/C=487-512 |
| 9DRX | EM | 2.95 Å | A/C=25-331, A/C=487-512 |
| 8SI9 | EM | 2.98 Å | A/C=25-331, A/C=486-512 |
| 7T0W | EM | 3.0 Å | A/C=25-331, A/C=488-511 |
| 7T0Z | EM | 3.0 Å | A/C=25-331, A/C=488-511 |
| 9CXA | EM | 3.04 Å | A=1-512 |
| 6X3S | EM | 3.12 Å | A/C=25-331, A/C=487-512 |
| 9CRV | EM | 3.18 Å | A/D=25-512 |
| 9CT0 | EM | 3.19 Å | A/C=25-512 |
| 6X3Z | EM | 3.23 Å | A/C=25-331, A/C=487-512 |
| 6X3W | EM | 3.3 Å | A/C=25-331, A/C=487-512 |
Showing 20 of 31 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.