Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (GNAS) is a 394-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63092.
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The mean pLDDT of this model is 91.3 (very high 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 | 78% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs) (PubMed:12391161, PubMed:17110384, PubMed:21488135, PubMed:26206488, PubMed:8702665, PubMed:10200251). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:12391161, PubMed:17110384, PubMed:10200251). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:12391161, PubMed:17110384, PubMed:10200251). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal…
Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Component of the TAS2R14-GNAS2 complex, consisting of TAS2R14, GNAS2, GNB1 and GNG2; within the complex interacts with TAS2R14; this complex plays a role in the perception of bitterness (PubMed:38776963). Interacts with CRY1; the interaction may block…
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7BPH | X-ray | 1.57 Å | A=7-394 |
| 6AU6 | X-ray | 1.7 Å | A=7-394 |
| 8F0K | EM | 1.9 Å | A=1-394 |
| 7E5E | X-ray | 1.95 Å | A/B/C/D=35-394 |
| 7MBX | EM | 1.95 Å | A=1-394 |
| 8F0J | EM | 2.0 Å | A=1-394 |
| 8F2B | EM | 2.0 Å | A=1-394 |
| 9XXT | EM | 2.0 Å | A=9-394 |
| 6X18 | EM | 2.1 Å | A=1-394 |
| 6X19 | EM | 2.1 Å | A=1-394 |
| 7RTB | EM | 2.14 Å | A=1-394 |
| 7TYF | EM | 2.2 Å | A=1-394 |
| 8F2A | EM | 2.2 Å | A=1-394 |
| 9BP3 | EM | 2.2 Å | A=1-394 |
| 9MZE | EM | 2.2 Å | A=1-394 |
| 9N05 | EM | 2.2 Å | A=1-394 |
| 6UVA | EM | 2.3 Å | A=1-394 |
| 6WZG | EM | 2.3 Å | A=1-394 |
| 8E3X | EM | 2.3 Å | A=1-394 |
| 8E3Y | EM | 2.3 Å | A=1-394 |
Showing 20 of 478 experimental structures (best resolution first).
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