Ras-related GTP-binding protein C (RRAGC) is a 399-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9HB90.
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The mean pLDDT of this model is 68.8 (low 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 | 7% |
| 70 to 90 | Confident: backbone generally right | 54% |
| 50 to 70 | Low: treat with caution | 15% |
| Below 50 | Very low: often disordered regions | 24% |
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:27234373, PubMed:31601708, PubMed:31601764, PubMed:32612235, PubMed:34071043, PubMed:36697823, PubMed:37057673). Forms heterodimeric Rag complexes with RagA/RRAGA or RagB/RRAGB and cycles between an inactive GTP-bound and an active GDP-bound form: RagC/RRAGC is in its active form when GDP-bound RagC/RRAGC forms a complex with GTP-bound RagA/RRAGA (or RagB/RRAGB) and in an inactive form when GTP-bound RagC/RRAGC heterodimerizes with GDP-bound RagA/RRAGA (or RagB/RRAGB) (PubMed:24095279,…
Forms a heterodimer with RRAGA, in a sequence-independent manner, and RRAGB (PubMed:11073942, PubMed:14660641, PubMed:32868926). Heterodimerization stabilizes proteins of the heterodimer (PubMed:11073942). The GDP-bound form of RRAGC (in complex with the GTP-bound form of RRAGA or RRAGB), interacts with RPTOR, thereby promoting recruitment of mTORC1 to the lysosomes (PubMed:18497260,…
Cytoplasm, Nucleus, Lysosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3LLU | X-ray | 1.4 Å | A=60-237 |
| 6S6D | X-ray | 2.5 Å | C/D=1-399 |
| 6S6A | X-ray | 2.63 Å | C/D=1-399 |
| 6EHR | X-ray | 2.9 Å | G=239-399 |
| 7UX2 | EM | 2.9 Å | C/J=1-399 |
| 6U62 | EM | 3.18 Å | C=2-399 |
| 6WJ2 | EM | 3.2 Å | G=1-399 |
| 7UXC | EM | 3.2 Å | E/L=1-399 |
| 7UXH | EM | 3.2 Å | G/N/W/d=1-399 |
| 9ED4 | EM | 3.23 Å | E/V=1-399 |
| 6ULG | EM | 3.31 Å | G=1-399 |
| 8DHB | EM | 3.53 Å | A=1-399 |
| 6NZD | EM | 3.6 Å | G=1-399 |
| 6WJ3 | EM | 3.9 Å | G=1-399 |
| 7T3B | EM | 3.9 Å | E=1-399 |
| 9ED6 | EM | 3.98 Å | C=1-399 |
| 6CES | EM | 4.0 Å | C=1-399 |
| 7T3A | EM | 4.0 Å | L=1-399 |
| 7T3C | EM | 4.0 Å | E/L=1-399 |
| 6SB0 | EM | 5.5 Å | D/J=1-399 |
Showing 20 of 21 experimental structures (best resolution first).
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