E3 ubiquitin-protein ligase UHRF1 (UHRF1) is a 793-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96T88.
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The mean pLDDT of this model is 79.8 (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 | 46% |
| 70 to 90 | Confident: backbone generally right | 31% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification (PubMed:10646863, PubMed:15009091, PubMed:19056828, PubMed:23022729, PubMed:24013172, PubMed:27595565, PubMed:30104358, PubMed:30392929, PubMed:30392931, PubMed:39607687). Plays a key role in DNA methylation inheritance by promoting recruitment of DNMT1 to hemimethylated DNA and ensure faithful propagation of the DNA methylation patterns through DNA replication (PubMed:23022729, PubMed:24013172, PubMed:27595565, PubMed:30104358, PubMed:30392929, PubMed:30392931, PubMed:39607687). Acts both as a histone reader and writer: specifically recognizes and binds (1)…
Interacts with DNMT1; the interaction is direct (PubMed:17673620, PubMed:21745816). Interacts with DNMT3A and DNMT3B (By similarity). Interacts with HDAC1, but not with HDAC2 (PubMed:15361834). Interacts with BLTP3A (PubMed:15361834). Interacts with EHMT2 (PubMed:19056828). Interacts with ZNF263; recruited to the SIX3 promoter along with other proteins involved in chromatin modification and…
Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6W92 | X-ray | 1.3 Å | A=122-283 |
| 6VYJ | X-ray | 1.39 Å | A=122-283 |
| 3ASL | X-ray | 1.41 Å | A=298-367 |
| 3ZVZ | X-ray | 1.45 Å | B=314-367 |
| 7FB7 | X-ray | 1.45 Å | A/B=123-285 |
| 8XV6 | X-ray | 1.6 Å | A/C=298-367 |
| 6B9M | X-ray | 1.68 Å | D=638-678 |
| 3BI7 | X-ray | 1.7 Å | A=414-617 |
| 5YYA | X-ray | 1.7 Å | A=123-285 |
| 6IIW | X-ray | 1.7 Å | A=299-366 |
| 6VCS | X-ray | 1.7 Å | A/B/E=414-617 |
| 3FL2 | X-ray | 1.75 Å | A=672-793 |
| 3SHB | X-ray | 1.8 Å | A=298-366 |
| 3SOU | X-ray | 1.8 Å | A/B=298-367 |
| 2PB7 | X-ray | 1.9 Å | A=408-643 |
| 3DWH | X-ray | 1.95 Å | A=414-617 |
| 3SOW | X-ray | 1.95 Å | A/B=298-367 |
| 3T6R | X-ray | 1.95 Å | A/B=299-364 |
| 3ZVY | X-ray | 1.95 Å | A/B=296-367 |
| 2FAZ | X-ray | 2.0 Å | A/B=1-76 |
Showing 20 of 45 experimental structures (best resolution first).
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