O15047: Histone-lysine N-methyltransferase SETD1A (SETD1A)

Histone-lysine N-methyltransferase SETD1A (SETD1A) is a 1707-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O15047.

Gene
SETD1A
Organism
Homo sapiens
Length
1707 residues
Mean pLDDT
48.3
Model
AF-O15047-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 48.3 (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 accurate9%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions69%

What pLDDT means and how to read it

Function

Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism (PubMed:12670868, PubMed:25561738). Part of chromatin remodeling machinery, forms H3K4me1, H3K4me2 and H3K4me3 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:29937342, PubMed:31197650, PubMed:32346159). Responsible for H3K4me3 enriched promoters and transcriptional programming of inner mass stem cells and neuron progenitors during embryogenesis (By similarity) (PubMed:31197650). Required for H3K4me1 mark at stalled replication forks. Mediates FANCD2-dependent…

Subunit structure

Component of the SET1A/COMPASS complex composed of the catalytic subunit SETD1A, WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 homotrimer (PubMed:16253997, PubMed:17355966, PubMed:17998332, PubMed:18838538, PubMed:22266653, PubMed:22665483, PubMed:23508102). Forms a core complex with the evolutionary conserved subcomplex WRAD composed of WDR5, RBBP5, ASH2L/ASH2 and DPY30 subunits;…

Subcellular location

Nucleus speckle, Chromosome, Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3S8SX-ray1.3 ÅA=89-197
4EWRX-ray1.5 ÅC=1488-1501
8ILYX-ray1.7 ÅA/B=89-195
3UVNX-ray1.79 ÅB/D=1492-1502

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