Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (GNAS) is a 394-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04896.
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The mean pLDDT of this model is 91.2 (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 | 79% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 3% |
| 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) (Probable) (PubMed:11087399, PubMed:2022671, PubMed:9395396). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (Probable) (PubMed:11087399, PubMed:2022671, PubMed:9395396). Signaling by an activated GPCR promotes GDP release and GTP binding (Probable) (PubMed:11087399, PubMed:2022671, PubMed:9395396). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (Probable) (PubMed:11087399,…
Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site (PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146, PubMed:9395396, PubMed:9417641). Component of the TAS2R14-GNAS2 complex, consisting of TAS2R14, GNAS2, GNB1 and GNG2; within the complex interacts with TAS2R14; this complex…
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1AZS | X-ray | 2.3 Å | C=1-394 |
| 1AZT | X-ray | 2.3 Å | A/B=1-394 |
| 9IJE | EM | 2.34 Å | A=26-394 |
| 1CUL | X-ray | 2.4 Å | C=1-394 |
| 1CS4 | X-ray | 2.5 Å | C=1-394 |
| 8DCS | EM | 2.5 Å | A=1-394 |
| 7JJO | EM | 2.6 Å | A=1-394 |
| 8DCR | EM | 2.6 Å | A=1-394 |
| 3C14 | X-ray | 2.68 Å | C=1-394 |
| 7VQX | EM | 2.74 Å | A=1-394 |
| 8X9T | EM | 2.75 Å | A=1-394 |
| 9IJD | EM | 2.76 Å | A=26-394 |
| 3C15 | X-ray | 2.78 Å | C=1-394 |
| 1CJT | X-ray | 2.8 Å | C=1-394 |
| 1CJU | X-ray | 2.8 Å | C=1-394 |
| 1TL7 | X-ray | 2.8 Å | C=1-394 |
| 8WA3 | EM | 2.86 Å | A=1-394 |
| 3C16 | X-ray | 2.87 Å | C=1-394 |
| 1U0H | X-ray | 2.9 Å | C=1-394 |
| 2GVD | X-ray | 2.9 Å | C=1-394 |
Showing 20 of 49 experimental structures (best resolution first).
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