Ras-related GTP-binding protein A (RRAGA) is a 313-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q7L523.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 92.5 (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 | 89% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade (PubMed:20381137, PubMed:24095279, PubMed:25936802, PubMed:31601708, PubMed:31601764, PubMed:38103557). Forms heterodimeric Rag complexes with RagC/RRAGC or RagD/RRAGD and cycles between an inactive GDP-bound and an active GTP-bound form: RagA/RRAGA is in its active form when GTP-bound RagA/RRAGA forms a complex with GDP-bound RagC/RRAGC (or RagD/RRAGD) and in an inactive form when GDP-bound RagA/RRAGA heterodimerizes with GTP-bound RagC/RRAGC (or RagD/RRAGD) (PubMed:20381137, PubMed:24095279, PubMed:25936802, PubMed:31601708,…
Can occur as a homodimer or as a heterodimer with RRAGC or RRAGD in a sequence-independent manner; heterodimerization stabilizes proteins of the heterodimer (PubMed:11073942, PubMed:20381137, PubMed:31601708, PubMed:31601764, PubMed:32868926). The GTP-bound form of RRAGA (in complex with the GDP-bound form of RRAGC or RRAGD) interacts with RPTOR, thereby promoting recruitment of mTORC1 to the…
Cytoplasm, Nucleus, Lysosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5X6V | X-ray | 2.02 Å | F=183-313 |
| 6S6D | X-ray | 2.5 Å | A/B=1-313 |
| 6S6A | X-ray | 2.63 Å | A/B=1-313 |
| 6EHR | X-ray | 2.9 Å | F=183-313 |
| 7UX2 | EM | 2.9 Å | B/I=1-313 |
| 6U62 | EM | 3.18 Å | B=1-313 |
| 6WJ2 | EM | 3.2 Å | F=1-313 |
| 7UXC | EM | 3.2 Å | D/K=1-313 |
| 7UXH | EM | 3.2 Å | F/M/V/c=1-313 |
| 9ED4 | EM | 3.23 Å | D/P=1-313 |
| 6ULG | EM | 3.31 Å | F=1-313 |
| 8DHB | EM | 3.53 Å | B=1-313 |
| 6NZD | EM | 3.6 Å | F=1-313 |
| 6WJ3 | EM | 3.9 Å | F=1-313 |
| 7T3B | EM | 3.9 Å | D=1-313 |
| 9ED6 | EM | 3.98 Å | B=1-313 |
| 6CES | EM | 4.0 Å | A=1-313 |
| 7T3A | EM | 4.0 Å | K=1-313 |
| 7T3C | EM | 4.0 Å | D/K=1-313 |
| 6SB0 | EM | 5.5 Å | C/I=1-313 |
Showing 20 of 21 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.