Q92800: Histone-lysine N-methyltransferase EZH1 (EZH1)

Histone-lysine N-methyltransferase EZH1 (EZH1) is a 747-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92800.

Gene
EZH1
Organism
Homo sapiens
Length
747 residues
Mean pLDDT
74.6
Model
AF-Q92800-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.6 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate38%
70 to 90Confident: backbone generally right30%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions21%

What pLDDT means and how to read it

Function

Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell derivation and self-renewal, suggesting that it is involved in safeguarding embryonic stem cell identity. Compared to EZH2-containing complexes, it is less abundant in embryonic stem cells, has weak methyltransferase activity and plays a less critical role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation

Subunit structure

Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2 (PubMed:19026781). The PRC2/EED-EZH1 is less abundant than the PRC2/EED-EZH2 complex, has weak methyltransferase activity and compacts chromatin in the absence of the methyltransferase cofactor S-adenosyl-L-methionine (SAM) (PubMed:19026781). Interacts with EZHIP; the interaction blocks EZH1…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7TD5X-ray2.99 ÅA/F=1-747
7KSOEM3.9 ÅA=1-747
7KSREM4.1 ÅA=1-747
7KTPEM4.8 ÅA=1-747

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