Guanine nucleotide-binding protein G(q) subunit alpha (GNAQ) is a 359-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P50148.
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The mean pLDDT of this model is 93.0 (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 | 84% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades (PubMed:34556863, PubMed:35672283, PubMed:37991948). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:37991948). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:37991948). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:37991948). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:37991948). Signaling is…
G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site (PubMed:37991948). Interacts (GDP-bound form) with RIC8A (via C-terminus); promoting GNAQ folding and association with the plasma membrane (PubMed:32126208). Binds NHERF1 (PubMed:12193606). Forms a complex with PECAM1 and BDKRB2 (PubMed:18672896). Interacts with GAS2L2…
Cell membrane, Golgi apparatus, Nucleus, Nucleus membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9M1H | EM | 2.55 Å | B=355-359 |
| 8THK | EM | 2.6 Å | A=355-359 |
| 8G59 | EM | 2.64 Å | A=335-359 |
| 8XGO | EM | 2.68 Å | E=25-359 |
| 9K27 | EM | 2.68 Å | E=25-359 |
| 9LL9 | EM | 2.76 Å | A=355-359 |
| 7F6I | EM | 2.8 Å | B=2-359 |
| 8YYX | EM | 2.84 Å | C=335-359 |
| 7EZM | EM | 2.9 Å | A=37-359 |
| 7F6G | EM | 2.9 Å | B=2-359 |
| 7F6H | EM | 2.9 Å | B=2-359 |
| 8Y52 | EM | 2.9 Å | A=7-359 |
| 8JPE | EM | 2.91 Å | Q=37-359 |
| 8IYS | EM | 2.95 Å | A=36-359 |
| 8XGS | EM | 2.95 Å | E=25-359 |
| 9LLB | EM | 2.98 Å | A=355-359 |
| 7W3Z | EM | 3.0 Å | B=36-359 |
| 7W40 | EM | 3.0 Å | B=36-359 |
| 8ZJD | EM | 3.06 Å | A=37-359 |
| 8JPB | EM | 3.07 Å | Q=37-359 |
Showing 20 of 36 experimental structures (best resolution first).
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