Histone-lysine N-methyltransferase SETDB1 (SETDB1) is a 1291-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15047.
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The mean pLDDT of this model is 65.1 (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 | 31% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 42% |
What pLDDT means and how to read it
Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) (PubMed:11959841, PubMed:12869583, PubMed:14536086, PubMed:27237050, PubMed:39096901). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones (PubMed:11959841, PubMed:12869583, PubMed:14536086, PubMed:27237050, PubMed:39096901). Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes (PubMed:12869583, PubMed:14536086, PubMed:27237050, PubMed:39096901). H3 'Lys-9' trimethylation is coordinated with DNA methylation (PubMed:12869583,…
Part of a complex containing at least CDYL, REST, WIZ, SETDB1, EHMT1 and EHMT2 (PubMed:19061646). Forms a complex with ATRX, TRIM28 and ZNF274 (PubMed:27029610). Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1 (PubMed:24623306). Interacts with TRIM28/TIF1B (PubMed:11959841). Interacts with ATF7IP and ATF7IP2; the interaction with ATF7IP protects SETDB1 from…
Nucleus, Cytoplasm, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6BHD | X-ray | 1.25 Å | A=190-410 |
| 9CUX | X-ray | 1.27 Å | A=196-403 |
| 6BHE | X-ray | 1.35 Å | A=190-410 |
| 6BHI | X-ray | 1.4 Å | A=190-410 |
| 6BHG | X-ray | 1.45 Å | A=190-410 |
| 5KCO | X-ray | 1.47 Å | A=196-403 |
| 9CUW | X-ray | 1.53 Å | A=196-403 |
| 5KE2 | X-ray | 1.56 Å | A=196-402 |
| 5QT1 | X-ray | 1.58 Å | A=196-397 |
| 5QT2 | X-ray | 1.59 Å | A=196-397 |
| 4X3S | X-ray | 1.6 Å | C/D=1165-1174 |
| 7CD9 | X-ray | 1.6 Å | A/B=190-410 |
| 6AU2 | X-ray | 1.63 Å | A=196-402 |
| 6BPI | X-ray | 1.64 Å | A=196-402 |
| 5KCH | X-ray | 1.7 Å | A=196-403 |
| 5KE3 | X-ray | 1.7 Å | A=196-402 |
| 3DLM | X-ray | 1.77 Å | A=196-402 |
| 8UWP | X-ray | 1.77 Å | A/B=196-403 |
| 6AU3 | X-ray | 1.8 Å | A=196-402 |
| 6BHH | X-ray | 1.85 Å | A=190-410 |
Showing 20 of 26 experimental structures (best resolution first).
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