Ragulator complex protein LAMTOR3 (LAMTOR3) is a 124-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UHA4.
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The mean pLDDT of this model is 95.5 (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 | 92% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (PubMed:20381137, PubMed:22980980, PubMed:28935770, PubMed:29107538, PubMed:29123114, PubMed:29158492, PubMed:30181260). Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator plays a dual role for the small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD): it (1) acts as a guanine nucleotide exchange factor (GEF), activating the small GTPases Rag and (2) mediates recruitment of Rag GTPases to the lysosome membrane (PubMed:22053050,…
Part of the Ragulator complex composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5 (PubMed:20381137, PubMed:22980980, PubMed:28935770, PubMed:29107538, PubMed:29123114, PubMed:29158492, PubMed:29285400, PubMed:31601708, PubMed:32868926, PubMed:35338845, PubMed:36103527, PubMed:36697823). LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3…
Late endosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6B9X | X-ray | 1.42 Å | C=1-124 |
| 3CPT | X-ray | 1.9 Å | A=2-124 |
| 1SKO | X-ray | 2.0 Å | A=2-124 |
| 2ZL1 | X-ray | 2.0 Å | A=2-124 |
| 5X6V | X-ray | 2.02 Å | A=2-124 |
| 6EHP | X-ray | 2.3 Å | A=1-124 |
| 5X6U | X-ray | 2.4 Å | A=2-124 |
| 5Y39 | X-ray | 2.65 Å | C/H=1-124 |
| 5Y3A | X-ray | 2.9 Å | C/H=1-124 |
| 6EHR | X-ray | 2.9 Å | A=1-124 |
| 7UX2 | EM | 2.9 Å | F/M=1-124 |
| 5YK3 | X-ray | 3.01 Å | D/H/m=1-124 |
| 6U62 | EM | 3.18 Å | F=1-124 |
| 6WJ2 | EM | 3.2 Å | C=1-124 |
| 7UXC | EM | 3.2 Å | H/O=1-124 |
| 7UXH | EM | 3.2 Å | J/Q/Z/g=1-124 |
| 9ED4 | EM | 3.23 Å | H/R=1-124 |
| 6ULG | EM | 3.31 Å | A=1-124 |
| 8DHB | EM | 3.53 Å | E=1-124 |
| 6NZD | EM | 3.6 Å | C=1-124 |
Showing 20 of 25 experimental structures (best resolution first).
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