Histone-lysine N-methyltransferase EZH2 (EZH2) is a 746-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15910.
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The mean pLDDT of this model is 76.3 (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 | 44% |
| 70 to 90 | Confident: backbone generally right | 25% |
| 50 to 70 | Low: treat with caution | 11% |
| Below 50 | Very low: often disordered regions | 21% |
What pLDDT means and how to read it
Catalytic subunit of the PRC2/EED-EZH2 complex, a Polycomb group (PcG) complex that methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene (PubMed:14532106, PubMed:15225548, PubMed:15385962, PubMed:16618801, PubMed:16936726, PubMed:17344414, PubMed:22323599, PubMed:24474760, PubMed:26581166, PubMed:30026490, PubMed:30923826). Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively (PubMed:15231737, PubMed:17210787, PubMed:18285464, PubMed:22323599, PubMed:30923826). Displays a preference for substrates with less methylation, loses activity when progressively…
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. The PRC2 complex may also interact with DNMT1, DNMT3A, DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via the SUZ12 subunit. Interacts with HDAC1 and HDAC2. Binds ATRX…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5U5T | X-ray | 1.6 Å | C/D=39-68 |
| 7QK4 | X-ray | 1.6 Å | B=40-68 |
| 7QJG | X-ray | 1.8 Å | C/D=40-68 |
| 7QJU | X-ray | 1.8 Å | C/D=40-68 |
| 5H14 | X-ray | 1.9 Å | C/D=40-68 |
| 5H19 | X-ray | 1.9 Å | B=40-68 |
| 5U62 | X-ray | 1.9 Å | C/D=39-68 |
| 4MI0 | X-ray | 2.0 Å | A=520-746 |
| 4MI5 | X-ray | 2.0 Å | A=521-746 |
| 5WUK | X-ray | 2.03 Å | B=41-68 |
| 6LO2 | X-ray | 2.21 Å | C/D=40-68 |
| 5H15 | X-ray | 2.27 Å | C/D=40-68 |
| 5H17 | X-ray | 2.3 Å | B=40-68 |
| 5GSA | X-ray | 2.49 Å | C/D=40-68 |
| 5H24 | X-ray | 2.5 Å | C/D=40-68 |
| 5IJ7 | X-ray | 2.62 Å | A/B=1-12, A/B=511-531 |
| 5H25 | X-ray | 2.88 Å | C/D=40-68 |
| 6U4Y | X-ray | 2.91 Å | A/B/C=2-182, A/B/C=220-257 |
| 5HYN | X-ray | 2.95 Å | A/F/K/Q=1-746 |
| 5IJ8 | X-ray | 2.99 Å | A/B=429-487, A/B=511-531, A/B=533-746 |
Showing 20 of 38 experimental structures (best resolution first).
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