RuvB-like 1 (RUVBL1) is a 456-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y265.
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The mean pLDDT of this model is 87.6 (confident 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 | 68% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity (PubMed:17157868, PubMed:33205750). Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A (PubMed:14966270). This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription (PubMed:14966270). This complex may be required…
Forms homohexameric rings (PubMed:33205750). Can form a dodecamer with RUVBL2 made of two stacked hexameric rings; however, even though RUVBL1 and RUVBL2 are present in equimolar ratio, the oligomeric status of each hexamer is not known (PubMed:33205750). Oligomerization may regulate binding to nucleic acids and conversely, binding to nucleic acids may affect the dodecameric assembly.…
Nucleus matrix, Nucleus, nucleoplasm, Cytoplasm, Membrane, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Dynein axonemal particle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2C9O | X-ray | 2.2 Å | A/B/C=1-456 |
| 8QR1 | EM | 2.4 Å | E/I/L=1-456 |
| 9EMA | EM | 2.4 Å | A/B/C=1-456 |
| 6K0R | X-ray | 2.5 Å | A/B/C/G/H/I=2-126, A/B/C/G/H/I=234-456 |
| 9C57 | EM | 2.75 Å | A/C/E=1-456 |
| 2XSZ | X-ray | 3.0 Å | A/B/C=2-456 |
| 9CAE | EM | 3.07 Å | E/G/I=1-456 |
| 7ZI4 | EM | 3.2 Å | A/C/E=1-456 |
| 8X15 | EM | 3.2 Å | M/O/Q=1-456 |
| 8X19 | EM | 3.2 Å | M/O/Q=1-456 |
| 8X1C | EM | 3.2 Å | M/O/Q=1-456 |
| 8XVT | EM | 3.2 Å | A/C/E=1-456 |
| 9EMC | EM | 3.26 Å | A/B/C=1-456 |
| 9CA7 | EM | 3.35 Å | E/G/I=1-456 |
| 9GE5 | EM | 3.35 Å | A/B/C=2-454 |
| 7OLE | EM | 3.41 Å | A/C/E=1-456 |
| 9CAC | EM | 3.43 Å | E/G/I=1-456 |
| 9GCG | EM | 3.43 Å | A/B/C=1-456 |
| 9GEV | EM | 3.47 Å | A/B/C=1-456 |
| 9HPO | EM | 3.5 Å | A/B/C/G/H/I=1-451 |
Showing 20 of 36 experimental structures (best resolution first).
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