DNA (cytosine-5)-methyltransferase 3-like (DNMT3L) is a 386-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UJW3.
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The mean pLDDT of this model is 86.4 (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 | 68% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
Catalytically inactive regulatory factor of DNA methyltransferases that can either promote or inhibit DNA methylation depending on the context (By similarity). Essential for the function of DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their catalytic domain (PubMed:17687327). Acts by accelerating the binding of DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases (PubMed:17687327). Recognizes unmethylated histone H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by recruitment or activation of DNMT3 (PubMed:17687327). Plays a key role in embryonic stem cells and germ cells (By…
Homodimer (PubMed:17687327, PubMed:17713477). Heterotetramer composed of 1 DNMT3A homodimer and 2 DNMT3L subunits (DNMT3L-DNMT3A-DNMT3A-DNMT3L) (PubMed:17713477). Interacts with histone H3 (via N-terminus); interaction is strongly inhibited by methylation at lysine 4 (H3K4me) (PubMed:17687327). Interacts with EZH2; the interaction is direct (By similarity). Interacts with SPOCD1 (By similarity)
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6W8B | X-ray | 2.4 Å | B/C/I/J=178-386 |
| 6W8J | X-ray | 2.44 Å | B/C=178-386 |
| 6W89 | X-ray | 2.5 Å | B/C/H/I=178-386 |
| 6W8D | X-ray | 2.6 Å | B/C=178-386 |
| 5YX2 | X-ray | 2.65 Å | B/C=178-385 |
| 6KDB | X-ray | 2.86 Å | B/C=178-379 |
| 6KDT | X-ray | 2.87 Å | B/C=178-379 |
| 2QRV | X-ray | 2.89 Å | B/C/F/G=160-386 |
| 4U7T | X-ray | 2.9 Å | B/D=178-379 |
| 6KDA | X-ray | 2.91 Å | B/C=178-379 |
| 6KDP | X-ray | 2.93 Å | B/C=178-379 |
| 6U8W | X-ray | 2.95 Å | B/C=178-386 |
| 6U8X | X-ray | 2.95 Å | B/C=178-386 |
| 6BRR | X-ray | 2.97 Å | B/C=178-386 |
| 6U8V | X-ray | 3.0 Å | B/C=178-386 |
| 6U90 | X-ray | 3.0 Å | B/C=178-386 |
| 6U91 | X-ray | 3.0 Å | B/C=178-386 |
| 8XEE | X-ray | 3.03 Å | B/C=178-379 |
| 6U8P | X-ray | 3.05 Å | B/C=178-386 |
| 7X9D | X-ray | 3.08 Å | B/C=178-379 |
Showing 20 of 29 experimental structures (best resolution first).
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