Q96KQ7: Histone-lysine N-methyltransferase EHMT2 (EHMT2)

Histone-lysine N-methyltransferase EHMT2 (EHMT2) is a 1210-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96KQ7.

Gene
EHMT2
Organism
Homo sapiens
Length
1210 residues
Mean pLDDT
68.3
Model
AF-Q96KQ7-F1 v6
Model created
1 Aug 2025
PDB structures
34

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.3 (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 accurate44%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions39%

What pLDDT means and how to read it

Function

Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones (PubMed:11316813, PubMed:20084102). Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication (PubMed:22387026). Also weakly methylates 'Lys-27' of histone H3 (H3K27me) (PubMed:11316813). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these…

Subunit structure

Heterodimer; heterodimerizes with EHMT1/GLP (PubMed:16702210). Interacts with GFI1B and WIZ (PubMed:16688220, PubMed:16702210). Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR, L3MBTL2 and YAF2 (PubMed:12004135). Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2 (PubMed:21549307). Interacts with UHRF1…

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5VSCX-ray1.4 ÅA/B=916-1190
7XUDX-ray1.45 ÅA/B=913-1193
5JIYX-ray1.48 ÅA/B=916-1189
7X73X-ray1.49 ÅA/B=913-1193
8Z7CX-ray1.52 ÅA/B=913-1193
8Z7EX-ray1.54 ÅA/B=913-1193
8Z7DX-ray1.58 ÅA/B=913-1193
5VSEX-ray1.6 ÅA/B=917-1190
5JHNX-ray1.67 ÅA/B=916-1189
7XUCX-ray1.67 ÅA/B=913-1193
3K5KX-ray1.7 ÅA/B=913-1193
5T0KX-ray1.7 ÅA/B=913-1193
5JJ0X-ray1.72 ÅA/B=916-1189
5TTFX-ray1.72 ÅA/B/C/D=913-1193
5V9IX-ray1.74 ÅA/B/C/D=913-1193
2O8JX-ray1.8 ÅA/B/C/D=913-1193
7DCFX-ray1.8 ÅA/B=913-1193
9KLBX-ray1.81 ÅA/B=913-1193
5JINX-ray1.85 ÅA/B=916-1189
9WRIX-ray1.85 ÅC=881-893

Showing 20 of 34 experimental structures (best resolution first).

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