SNW domain-containing protein 1 (SNW1) is a 536-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13573.
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The mean pLDDT of this model is 78.5 (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 | 40% |
| 70 to 90 | Confident: backbone generally right | 28% |
| 50 to 70 | Low: treat with caution | 24% |
| Below 50 | Very low: often disordered regions | 8% |
What pLDDT means and how to read it
Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28076346, PubMed:28502770). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Required for the specific splicing of CDKN1A pre-mRNA; the function probably involves the recruitment of U2AF2 to the mRNA. May recruit PPIL1 to the spliceosome. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in transcriptional regulation. Modulates TGF-beta-mediated transcription via association with SMAD proteins, MYOD1-mediated transcription via association…
Identified in the spliceosome C complex (PubMed:11991638, PubMed:28076346, PubMed:28502770). Associates with U4/U6-U5 tri-small nuclear ribonucleoproteins (U4/U6-U5 tri-snRNPs). Component of the minor spliceosome, which splices U12-type introns (PubMed:33509932). Interacts with SKI, SMAD2,SMAD3, RBPJ, RB1, PABPN1, MAGEA1, SIRT1, FOXN3, U2AF2, DAXX and ATP1B4. Interacts with PPIL1…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8C6J | EM | 2.8 Å | K=1-536 |
| 6ID1 | EM | 2.86 Å | R=1-536 |
| 7DVQ | EM | 2.89 Å | R=1-536 |
| 6ID0 | EM | 2.9 Å | R=1-536 |
| 6ICZ | EM | 3.0 Å | R=1-536 |
| 8I0R | EM | 3.0 Å | R=1-536 |
| 8I0T | EM | 3.0 Å | R=1-536 |
| 8I0V | EM | 3.0 Å | R=1-536 |
| 7QTT | EM | 3.1 Å | Y=1-536 |
| 6QDV | EM | 3.3 Å | K=41-335 |
| 8I0U | EM | 3.3 Å | R=1-536 |
| 9FMD | EM | 3.3 Å | R=1-536 |
| 6ZYM | EM | 3.4 Å | C=1-536 |
| 8I0P | EM | 3.4 Å | R=1-536 |
| 8I0W | EM | 3.4 Å | R=1-536 |
| 8RO2 | EM | 3.5 Å | R=1-536 |
| 5XJC | EM | 3.6 Å | R=1-536 |
| 7W59 | EM | 3.6 Å | R=1-536 |
| 7W5A | EM | 3.6 Å | R=1-536 |
| 7ABF | EM | 3.9 Å | v=1-536 |
Showing 20 of 32 experimental structures (best resolution first).
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