Inactive histone-lysine N-methyltransferase 2E (KMT2E) is a 1858-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8IZD2.
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The mean pLDDT of this model is 44.0 (very 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 | 8% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 80% |
What pLDDT means and how to read it
Associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription (PubMed:23629655, PubMed:23798402, PubMed:24130829). Chromatin interaction is mediated via the binding to tri-methylated histone H3 at 'Lys-4' (H3K4me3) (PubMed:23798402, PubMed:24130829). Key regulator of hematopoiesis involved in terminal myeloid differentiation and in the regulation of hematopoietic stem cell (HSCs) self-renewal by a mechanism that involves DNA methylation (By similarity). Also acts as an important cell cycle regulator, participating in cell cycle regulatory network machinery at multiple cell cycle stages including G1/S transition, S phase…
Component of a complex composed of KMT2E (isoform 3), OGT and USP7; the complex stabilizes KMT2E, preventing KMT2E ubiquitination and proteasomal-mediated degradation (PubMed:26678539). Isoform 3 interacts (via N-terminus) with OGT (via TRP repeats) (PubMed:23629655, PubMed:26678539). Isoform 3 interacts with deubiquitinating enzyme USP7 (via MATH domain) (PubMed:26678539). Isoform 3 interacts…
Chromosome, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Nucleus speckle, Nucleus, nucleoplasm, Cytoplasm, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4L58 | X-ray | 1.48 Å | A=117-181 |
| 5HT6 | X-ray | 2.09 Å | A/B=323-458 |
| 2LV9 | NMR | A=109-188 |
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