O96028: Histone-lysine N-methyltransferase NSD2 (NSD2)

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.

Gene
NSD2
Organism
Homo sapiens
Length
1365 residues
Mean pLDDT
65.6
Model
AF-O96028-F1 v6
Model created
1 Aug 2025
PDB structures
22

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Model confidence (pLDDT)

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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate28%
70 to 90Confident: backbone generally right27%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions39%

What pLDDT means and how to read it

Function

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…

Subunit structure

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

Subcellular location

Nucleus, Chromosome, Cytoplasm, Nucleus, nucleolus

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
9FOCX-ray1.62 ÅA/B=208-368
6XCGX-ray1.64 ÅA/B/C=211-350
9EXYX-ray1.7 ÅA/B=208-368
9GBFX-ray1.76 ÅA/B=1229-1331
5VC8X-ray1.8 ÅA/B=211-350
9KNBX-ray1.84 ÅA=217-349
9EXXX-ray1.94 ÅA/B=208-368
9FOEX-ray1.96 ÅA=208-368
9KN9X-ray2.0 ÅA/B=217-349
5LSUX-ray2.14 ÅA/B=973-1203
7LMTX-ray2.27 ÅA/B/C/D/E/F/G/H=211-350
6UE6X-ray2.4 ÅA/B/C/D/E/F/G/H=211-350
7MDNX-ray2.42 ÅA/B/C/D/E/F/G/H=211-350
9EXWX-ray2.43 ÅA/B=208-368
7E8DEM2.8 ÅK=973-1226
9KNAX-ray2.92 ÅA/B=217-348
7VLNX-ray3.09 ÅA/B/C=217-348
7CROEM3.75 ÅI=661-1365
29HGEM4.0 ÅB=1-1365
29HHEM4.2 ÅB=1-1365

Showing 20 of 22 experimental structures (best resolution first).

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