GTP-binding protein Rheb (RHEB) is a 184-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15382.
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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 | 83% |
| 70 to 90 | Confident: backbone generally right | 10% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Small GTPase that acts as an allosteric activator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12842888, PubMed:12869586, PubMed:12906785, PubMed:15340059, PubMed:15854902, PubMed:16098514, PubMed:20381137, PubMed:22819219, PubMed:24529379, PubMed:29416044, PubMed:32470140, PubMed:33157014, PubMed:25816988). In response to nutrients, growth factors or amino acids, specifically activates the protein kinase activity of MTOR, the catalytic component of the mTORC1 complex: acts by causing a…
Associates with the mTORC1 complex (MTOR, MLST8 and RPTOR) in a guanyl nucleotide-independent manner (PubMed:15854902, PubMed:16098514, PubMed:24529379). Interacts with TSC2 (PubMed:15854902, PubMed:22819219, PubMed:24529379, PubMed:25816988). Interacts with MCRS1; the interaction maintains RHEB at the lysosome in its active GTP-bound form and prevents its interaction with the mTORC1 complex…
Endomembrane system, Lysosome membrane, Golgi apparatus membrane, Endoplasmic reticulum membrane, Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6BSX | X-ray | 1.65 Å | A/B/C/D=1-169 |
| 3T5G | X-ray | 1.7 Å | A=1-181 |
| 1XTQ | X-ray | 2.0 Å | A=1-169 |
| 3SEA | X-ray | 2.0 Å | A/B=3-169 |
| 7BTD | X-ray | 2.0 Å | A=1-169 |
| 5YXH | X-ray | 2.04 Å | A/B/C/D=2-169 |
| 7BTC | X-ray | 2.1 Å | A/B/C/D=1-169 |
| 6BT0 | X-ray | 2.6 Å | A/B/C/D=1-169 |
| 7BTA | X-ray | 2.6 Å | A/B=1-169 |
| 1XTR | X-ray | 2.65 Å | A=1-169 |
| 1XTS | X-ray | 2.8 Å | A=1-169 |
| 9ED7 | EM | 3.16 Å | L=1-184 |
| 9ED4 | EM | 3.23 Å | L/N=1-184 |
| 6BCU | EM | 3.43 Å | R/S=1-184 |
| 9ED8 | EM | 3.61 Å | L=1-184 |
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