Guanine nucleotide-binding protein G(i) subunit alpha-1 (Gnai1) is a 354-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P10824.
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The mean pLDDT of this model is 93.6 (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 | 85% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 2% |
| 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:19703466, PubMed:24596087, PubMed:25037222). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:19703466, PubMed:24596087, PubMed:25037222). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:19703466, PubMed:24596087, PubMed:25037222). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:21158412). Both GDP release and GTP hydrolysis are…
Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site (PubMed:24596087, PubMed:25037222, PubMed:8521505). Part of a spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1 (By similarity). Identified in complex with the beta subunit GNB1 and the gamma subunit GNG1 (PubMed:24596087). Identified in…
Cell membrane, Nucleus, Cytoplasm, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cytoplasm, cell cortex
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1CIP | X-ray | 1.5 Å | A=2-354 |
| 1SVS | X-ray | 1.5 Å | A=2-354 |
| 4N0D | X-ray | 1.55 Å | A=1-354 |
| 5KDO | X-ray | 1.9 Å | A=1-354 |
| 1AS0 | X-ray | 2.0 Å | A=2-354 |
| 1GIA | X-ray | 2.0 Å | A=2-354 |
| 1SVK | X-ray | 2.0 Å | A=2-354 |
| 4PAO | X-ray | 2.0 Å | A=1-354 |
| 4PAQ | X-ray | 2.0 Å | A=1-354 |
| 1FQJ | X-ray | 2.02 Å | A/D=220-299 |
| 6M8H | X-ray | 2.07 Å | A=1-354 |
| 1BH2 | X-ray | 2.1 Å | A=32-346 |
| 4N0E | X-ray | 2.1 Å | A=1-354 |
| 4PAM | X-ray | 2.1 Å | A=1-354 |
| 1BOF | X-ray | 2.2 Å | A=2-354 |
| 1GDD | X-ray | 2.2 Å | A=2-354 |
| 1GFI | X-ray | 2.2 Å | A=2-354 |
| 1FQK | X-ray | 2.3 Å | A/C=220-299 |
| 1GIL | X-ray | 2.3 Å | A=2-354 |
| 1GP2 | X-ray | 2.3 Å | A=2-354 |
Showing 20 of 44 experimental structures (best resolution first).
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