Guanine nucleotide-binding protein subunit beta-5 (GNB5) is a 395-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O14775.
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The mean pLDDT of this model is 94.0 (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 | 83% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Enhances GTPase-activating protein (GAP) activity of regulator of G protein signaling (RGS) proteins, such as RGS7 and RGS9, hence involved in the termination of the signaling initiated by the G protein-coupled receptors (GPCRs) by accelerating the GTP hydrolysis on the G-alpha subunits, thereby promoting their inactivation (PubMed:27677260). Increases RGS7 GTPase-activating protein (GAP) activity, thereby regulating mood and cognition (By similarity). Increases RGS9 GTPase-activating protein (GAP) activity, hence contributes to the deactivation of G protein signaling initiated by D(2) dopamine receptors (PubMed:27677260). May play an important role in neuronal signaling, including in the…
Component of a complex composed of RGS9 (isoform RGS9-1), GNB5 and RGS9BP; within this complex, the presence of GNB5 stabilizes both itself and RGS9 and increases RGS9 GTPase-activating protein (GAP) activity (PubMed:27677260). Interacts with RGS7, forming the RGS7-GNB5 complex; within this complex, the presence of GNB5 increases RGS7 GTPase-activating protein (GAP) activity (PubMed:34815401).…
Membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8SH9 | EM | 2.7 Å | N=1-395 |
| 8SHE | EM | 2.8 Å | N=1-395 |
| 8SHG | EM | 2.8 Å | N=1-395 |
| 8SHN | EM | 2.8 Å | N=1-395 |
| 8SG9 | EM | 2.9 Å | N=1-395 |
| 8SGC | EM | 2.9 Å | N=1-395 |
| 8SGL | EM | 2.9 Å | N=1-395 |
| 8SHD | EM | 2.9 Å | N=1-395 |
| 8SHQ | EM | 2.9 Å | N=1-395 |
| 9NOQ | EM | 2.9 Å | N=1-395 |
| 9NRH | EM | 2.9 Å | N=1-395 |
| 8SG8 | EM | 3.0 Å | N=1-395 |
| 8SHA | EM | 3.0 Å | N=1-395 |
| 8SHF | EM | 3.0 Å | N=1-395 |
| 8SHL | EM | 3.0 Å | N=1-395 |
| 8SHO | EM | 3.0 Å | N=1-395 |
| 8SHP | EM | 3.0 Å | N=1-395 |
| 8SHT | EM | 3.0 Å | N=1-395 |
| 9NPW | EM | 3.0 Å | N=1-395 |
| 9NQ1 | EM | 3.0 Å | N=1-395 |
Showing 20 of 32 experimental structures (best resolution first).
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