Sequestosome-1 (Sqstm1) is a 442-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q64337.
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The mean pLDDT of this model is 66.9 (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 | 30% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 14% |
| Below 50 | Very low: often disordered regions | 36% |
What pLDDT means and how to read it
Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:25723488, PubMed:33397898, PubMed:37306101). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:25723488, PubMed:33397898). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:33397898). SQSTM1 then interacts with ATG8…
Homooligomer or heterooligomer; may form homotypic arrays (PubMed:20173742). Dimerization interferes with ubiquitin binding (By similarity). Component of a ternary complex with PAWR and PRKCZ (By similarity). Forms a complex with JUB/Ajuba, PRKCZ and TRAF6 (By similarity). Identified in a complex with TRAF6 and CYLD (PubMed:18382763). Identified in a heterotrimeric complex with ubiquitin and…
Cytoplasmic vesicle, autophagosome, Preautophagosomal structure, Cytoplasm, cytosol, Nucleus, PML body, Late endosome, Lysosome, Nucleus, Endoplasmic reticulum, Cytoplasm, myofibril, sarcomere
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3B0F | X-ray | 1.4 Å | A/B=391-438 |
| 2ZJD | X-ray | 1.56 Å | B/D=334-344 |
| 3WDZ | X-ray | 2.6 Å | B=346-359 |
| 3ADE | X-ray | 2.8 Å | B=346-359 |
| 2RRU | NMR | A=391-438 |
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