Protein PALS1 (PALS1) is a 675-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8N3R9.
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The mean pLDDT of this model is 77.2 (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 | 48% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 20% |
What pLDDT means and how to read it
Plays a role in tight junction biogenesis and in the establishment of cell polarity in epithelial cells (PubMed:16678097, PubMed:25385611). Also involved in adherens junction biogenesis by ensuring correct localization of the exocyst complex protein EXOC4/SEC8 which allows trafficking of adherens junction structural component CDH1 to the cell surface (By similarity). Plays a role through its interaction with CDH5 in vascular lumen formation and endothelial membrane polarity (PubMed:27466317). Required during embryonic and postnatal retinal development (By similarity). Required for the maintenance of cerebellar progenitor cells in an undifferentiated proliferative state, preventing…
Heterodimer with MPP1 (PubMed:17584769). Forms a heterotrimeric complex composed of PALS1, LIN7B and PATJ; the N-terminal L27 domain of PALS1 interacts with the L27 domain of PATJ and the C-terminal L27 domain of PALS1 interacts with the L27 domain of LIN7B (PubMed:22337881). Component of a complex composed of PALS1, CRB1 and MPP4 (PubMed:15914641). Component of a complex whose core is composed…
Golgi apparatus, Cell membrane, Endomembrane system, Cell junction, tight junction, Cell junction, adherens junction, Cell projection, axon, Perikaryon, Apical cell membrane, Endoplasmic reticulum-Golgi intermediate compartment
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4UU5 | X-ray | 1.23 Å | A=251-335 |
| 7NTJ | X-ray | 1.74 Å | A/B=255-336 |
| 4UU6 | X-ray | 1.8 Å | A=251-335 |
| 7NTK | X-ray | 1.9 Å | A/B/D/F=255-336 |
| 3UIT | X-ray | 2.05 Å | A/B/C/D=119-232 |
| 7QCS | X-ray | 2.8 Å | A/B/E=238-336 |
| 4WSI | X-ray | 2.95 Å | A/B=236-675 |
| 7M4R | EM | 3.65 Å | A/B=236-675 |
| 1Y76 | NMR | B/D=118-177 |
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