Speckle-type POZ protein (SPOP) is a 374-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43791.
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The mean pLDDT of this model is 90.1 (very high 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 | 77% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. In complex with CUL3, involved in ubiquitination and proteasomal degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with CUL3, involved in ubiquitination of MACROH2A1 and BMI1; this does not lead to their proteasomal degradation. Inhibits transcriptional activation of PDX1/IPF1 targets, such as insulin, by promoting PDX1/IPF1 degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOP has higher ubiquitin ligase activity than…
Interacts with GLI2 and GLI3 (By similarity). Homodimer and homooligomer. Heterodimer with SPOPL. Each dimer interacts with two CUL3 molecules. Part of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that contain CUL3 and homodimeric SPOP, or the heterodimer formed by SPOP and SPOPL, plus a target protein, such as MACROH2A1, PDX1/IPF1, BMI1, BRMS1 and DAXX. Interacts…
Nucleus, Nucleus speckle, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3IVV | X-ray | 1.25 Å | A=28-166 |
| 3HSV | X-ray | 1.43 Å | A/B=28-166 |
| 7LIN | X-ray | 1.44 Å | A=29-166 |
| 7D3D | X-ray | 1.45 Å | A/B=28-166 |
| 9HFV | X-ray | 1.45 Å | A=28-166 |
| 7LIP | X-ray | 1.48 Å | A=29-166 |
| 4HS2 | X-ray | 1.53 Å | A=270-374 |
| 3HQL | X-ray | 1.66 Å | A/B=28-166 |
| 3HQM | X-ray | 1.74 Å | A/B=28-166 |
| 3IVB | X-ray | 1.75 Å | A=28-166 |
| 6I5P | X-ray | 1.81 Å | A/C/E/G=28-166 |
| 6I68 | X-ray | 1.85 Å | A/C/E/G=28-166 |
| 6I41 | X-ray | 1.9 Å | A=28-166 |
| 9HGG | X-ray | 1.9 Å | A=28-166 |
| 7LIQ | X-ray | 1.98 Å | A=29-166 |
| 4O1V | X-ray | 2.0 Å | A=28-166 |
| 6F8F | X-ray | 2.0 Å | D=28-166 |
| 6F8G | X-ray | 2.03 Å | A/B/C/D=28-166 |
| 3IVQ | X-ray | 2.1 Å | A/B=28-166 |
| 6I7A | X-ray | 2.2 Å | A/C/E/G=28-166 |
Showing 20 of 36 experimental structures (best resolution first).
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