Polycomb protein EED (EED) is a 441-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75530.
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The mean pLDDT of this model is 86.5 (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 | 79% |
| 70 to 90 | Confident: backbone generally right | 3% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A
Component of the PRC2/EED-EZH2 complex, which includes EED, EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2. The minimum components required for methyltransferase activity of the PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. The PRC2 complex may also interact with DNMT1, DNMT3A, DNMT3B and PHF1 via the…
Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5U69 | X-ray | 1.28 Å | A=77-441 |
| 5U8F | X-ray | 1.34 Å | A=77-441 |
| 5U8A | X-ray | 1.45 Å | A=77-441 |
| 6SFB | X-ray | 1.52 Å | A/B=76-441 |
| 3K26 | X-ray | 1.58 Å | A=76-441 |
| 5U5T | X-ray | 1.6 Å | A/B=76-441 |
| 7QK4 | X-ray | 1.6 Å | A=77-441 |
| 7P3C | X-ray | 1.61 Å | A/B=76-441 |
| 6V3Y | X-ray | 1.63 Å | A=81-439 |
| 5U6D | X-ray | 1.64 Å | A=77-441 |
| 6V3X | X-ray | 1.7 Å | A=75-441 |
| 5TTW | X-ray | 1.74 Å | A/C=76-441 |
| 7SI5 | X-ray | 1.75 Å | A=40-441 |
| 3K27 | X-ray | 1.76 Å | A=76-441 |
| 3IIW | X-ray | 1.8 Å | A=77-441 |
| 5U5H | X-ray | 1.8 Å | A=76-441 |
| 7QJG | X-ray | 1.8 Å | A/B=77-441 |
| 7QJU | X-ray | 1.8 Å | A/B=77-441 |
| 5K0M | X-ray | 1.83 Å | A=77-441 |
| 6YVJ | X-ray | 1.84 Å | A/B=76-441 |
Showing 20 of 78 experimental structures (best resolution first).
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