Mitochondrial assembly of ribosomal large subunit protein 1 (MALSU1) is a 234-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96EH3.
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The mean pLDDT of this model is 69.3 (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 | 40% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 39% |
What pLDDT means and how to read it
Required for normal mitochondrial ribosome function and mitochondrial translation (PubMed:22238375, PubMed:23171548). May play a role in ribosome biogenesis by preventing premature association of the 28S and 39S ribosomal subunits (Probable). Interacts with mitochondrial ribosomal protein uL14m (MRPL14), probably blocking formation of intersubunit bridge B8, preventing association of the 28S and 39S ribosomal subunits (Probable). Addition to isolated mitochondrial ribosomal subunits partially inhibits translation, probably by interfering with the association of the 28S and 39S ribosomal subunits and the formation of functional ribosomes (Probable). May also participate in the assembly…
Associates with the mitochondrial ribosome large subunit (39S) via interaction with MRPL12 and/or MRPL14 (PubMed:22238375, PubMed:23171548, PubMed:28892042, PubMed:35177605). The interaction generates steric hindrance that is expected to prevent premature association of the 28S and 39S ribosomal subunits (PubMed:28892042). Interacts with intermediates of the mitochondrial ribosome large subunit…
Mitochondrion matrix
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7OF0 | EM | 2.2 Å | u=1-234 |
| 8QU5 | EM | 2.42 Å | u=1-234 |
| 7O9M | EM | 2.5 Å | u=1-234 |
| 7OF7 | EM | 2.5 Å | u=1-234 |
| 7PO4 | EM | 2.56 Å | za=1-234 |
| 7OF2 | EM | 2.7 Å | u=1-234 |
| 7OF3 | EM | 2.7 Å | u=1-234 |
| 7QH7 | EM | 2.89 Å | u=91-201 |
| 7ODR | EM | 2.9 Å | u=1-234 |
| 7OF5 | EM | 2.9 Å | u=1-234 |
| 8QSJ | EM | 3.0 Å | u=1-234 |
| 5OOM | EM | 3.03 Å | u=1-234 |
| 8PK0 | EM | 3.03 Å | u=1-234 |
| 5OOL | EM | 3.06 Å | u=1-234 |
| 7QH6 | EM | 3.08 Å | u=1-234 |
| 7A5J | EM | 3.1 Å | u=1-234 |
| 7O9K | EM | 3.1 Å | u=1-234 |
| 7ODS | EM | 3.1 Å | u=1-234 |
| 7ODT | EM | 3.1 Å | u=1-234 |
| 7OIC | EM | 3.1 Å | u=1-234 |
Showing 20 of 29 experimental structures (best resolution first).
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