Ragulator complex protein LAMTOR5 (LAMTOR5) is a 91-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43504.
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The mean pLDDT of this model is 96.6 (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 | 95% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 1% |
| 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:22980980, 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, PubMed:22980980, PubMed:28935770, PubMed:29107538, PubMed:29158492,…
Homodimer (PubMed:21059355). Part of the Ragulator complex composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5 (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,…
Lysosome, Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6B9X | X-ray | 1.42 Å | E=1-91 |
| 3MSH | X-ray | 1.51 Å | A=1-91 |
| 5X6V | X-ray | 2.02 Å | C=1-91 |
| 5YK5 | X-ray | 2.03 Å | B/D=2-90 |
| 3MS6 | X-ray | 2.08 Å | A=1-91 |
| 6EHP | X-ray | 2.3 Å | C=1-91 |
| 5X6U | X-ray | 2.4 Å | C=1-91 |
| 5Y39 | X-ray | 2.65 Å | E/J=1-90 |
| 5Y38 | X-ray | 2.8 Å | A=1-91 |
| 5VOK | X-ray | 2.89 Å | A/C/E/G=1-91 |
| 5Y3A | X-ray | 2.9 Å | E/J=1-91 |
| 6EHR | X-ray | 2.9 Å | C=1-91 |
| 7UX2 | EM | 2.9 Å | H/O=1-91 |
| 5YK3 | X-ray | 3.01 Å | E/J=1-91, o=1-90 |
| 6U62 | EM | 3.18 Å | H=1-91 |
| 6WJ2 | EM | 3.2 Å | E=1-91 |
| 7UXC | EM | 3.2 Å | J/Q=1-91 |
| 7UXH | EM | 3.2 Å | L/S/b/i=1-91 |
| 9ED4 | EM | 3.23 Å | J/S=1-91 |
| 6ULG | EM | 3.31 Å | C=1-91 |
Showing 20 of 27 experimental structures (best resolution first).
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