Q2LAE1: Histone-lysine N-methyltransferase ASHH2 (ASHH2)

Histone-lysine N-methyltransferase ASHH2 (ASHH2) is a 1759-residue protein from Arabidopsis thaliana. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q2LAE1.

Gene
ASHH2
Organism
Arabidopsis thaliana
Length
1759 residues
Mean pLDDT
42.3
Model
AF-Q2LAE1-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 42.3 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate11%
70 to 90Confident: backbone generally right6%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions77%

What pLDDT means and how to read it

Function

Histone methyltransferase involved in di and tri-methylation of 'Lys-36' of histone H3 (H3K36me2 and H3K36me3). Binds to H3 already mono- or di-methylated on 'Lys-4'(H3K4me1 or H3K4me2), but not to H3K4me3. H3K4me and H3K36me represent specific tags for epigenetic transcriptional activation. Positively regulates FLC transcription to prevent early flowering transition. Required for flowering transition in response to vernalization and for the maintenance of FLC expression in late embryos, but dispensable for the initial reactivation in early embryos during reprogramming. Also seems to modulate several traits including floral organ size, root size and dormancy. Promotes apical dominance…

Subunit structure

Interacts with FRI and SUF4, two components of the transcription activator complex FRI-C, and with SWC6, a component of the SWR1 chromatin-remodeling complex (PubMed:20711170, PubMed:21282526, PubMed:21522130). Interacts with BZR2/BES1 and IWS1 (PubMed:24838002)

Subcellular location

Nucleus, Chromosome, centromere

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5YVXX-ray1.59 ÅA=862-921
2L7PNMRA=849-937
6QXZNMRA=861-928

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