Histone-lysine N-methyltransferase NSD2 (NSD2) is a 1365-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O96028.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 65.6 (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 | 28% |
| 70 to 90 | Confident: backbone generally right | 27% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 39% |
What pLDDT means and how to read it
Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2) (PubMed:19808676, PubMed:22099308, PubMed:27571355, PubMed:29728617, PubMed:33941880). Also monomethylates nucleosomal histone H3 at 'Lys-36' (H3K36me) in vitro (PubMed:22099308). Does not trimethylate nucleosomal histone H3 at 'Lys-36' (H3K36me3) (PubMed:22099308). However, specifically trimethylates histone H3 at 'Lys-36' (H3K36me3) at euchromatic regions in embryonic stem (ES) cells (By similarity). By methylating histone H3 at 'Lys-36', involved in the regulation of gene transcription during various biological processes (PubMed:16115125, PubMed:22099308, PubMed:29728617). In ES…
Interacts with HDAC1. Interacts (via PHD-type zinc fingers 1, 2 and 3) with SALL1. Interacts (via PHD-type 1, 2 and 3) with SALL4. Interacts with NANOG. Interacts with OGT. Interacts (via HMG box) with NKX2-5
Nucleus, Chromosome, Cytoplasm, Nucleus, nucleolus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9FOC | X-ray | 1.62 Å | A/B=208-368 |
| 6XCG | X-ray | 1.64 Å | A/B/C=211-350 |
| 9EXY | X-ray | 1.7 Å | A/B=208-368 |
| 9GBF | X-ray | 1.76 Å | A/B=1229-1331 |
| 5VC8 | X-ray | 1.8 Å | A/B=211-350 |
| 9KNB | X-ray | 1.84 Å | A=217-349 |
| 9EXX | X-ray | 1.94 Å | A/B=208-368 |
| 9FOE | X-ray | 1.96 Å | A=208-368 |
| 9KN9 | X-ray | 2.0 Å | A/B=217-349 |
| 5LSU | X-ray | 2.14 Å | A/B=973-1203 |
| 7LMT | X-ray | 2.27 Å | A/B/C/D/E/F/G/H=211-350 |
| 6UE6 | X-ray | 2.4 Å | A/B/C/D/E/F/G/H=211-350 |
| 7MDN | X-ray | 2.42 Å | A/B/C/D/E/F/G/H=211-350 |
| 9EXW | X-ray | 2.43 Å | A/B=208-368 |
| 7E8D | EM | 2.8 Å | K=973-1226 |
| 9KNA | X-ray | 2.92 Å | A/B=217-348 |
| 7VLN | X-ray | 3.09 Å | A/B/C=217-348 |
| 7CRO | EM | 3.75 Å | I=661-1365 |
| 29HG | EM | 4.0 Å | B=1-1365 |
| 29HH | EM | 4.2 Å | B=1-1365 |
Showing 20 of 22 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.