Target of rapamycin complex subunit LST8 (MLST8) is a 326-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BVC4.
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The mean pLDDT of this model is 91.6 (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 | 81% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073, PubMed:28489822). mTORC1 is activated in response to growth factors or amino acids (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073). In response to nutrients, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating several substrates, such as ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073). In the same time, it inhibits catabolic…
Part of the mechanistic target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8 and RPTOR (PubMed:12408816, PubMed:12718876, PubMed:15268862, PubMed:17510057, PubMed:23636326, PubMed:24403073, PubMed:26678875, PubMed:27909983, PubMed:28489822, PubMed:29236692, PubMed:31601764, PubMed:34519268, PubMed:34519269, PubMed:36697823). mTORC1 associates with AKT1S1/PRAS40, which inhibits its…
Lysosome membrane, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9T94 | EM | 2.6 Å | C=1-326 |
| 9ZBK | EM | 2.6 Å | B=7-324 |
| 8ERA | EM | 2.86 Å | C=1-326 |
| 9T93 | EM | 2.86 Å | C=1-326 |
| 6BCX | EM | 3.0 Å | D/E=1-326 |
| 6ZWO | EM | 3.0 Å | D=1-326 |
| 9T7J | EM | 3.0 Å | C/D=1-326 |
| 9TDT | EM | 3.0 Å | C=1-326 |
| 5WBY | X-ray | 3.1 Å | C/D=1-326 |
| 9T92 | EM | 3.1 Å | C/D=1-326 |
| 9ED7 | EM | 3.16 Å | B=1-326 |
| 4JSN | X-ray | 3.2 Å | C/D=1-326 |
| 6ZWM | EM | 3.2 Å | C/D=1-326 |
| 7PE8 | EM | 3.2 Å | C=1-326 |
| 7UXC | EM | 3.2 Å | B=1-326 |
| 7UXH | EM | 3.2 Å | B/D=1-326 |
| 9ZBJ | EM | 3.2 Å | B=7-323 |
| 9ED4 | EM | 3.23 Å | B/M=1-326 |
| 7TZO | EM | 3.28 Å | C/D=1-326 |
| 4JSP | X-ray | 3.3 Å | C/D=1-326 |
Showing 20 of 45 experimental structures (best resolution first).
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