Q9BYW2: Histone-lysine N-methyltransferase SETD2 (SETD2)

Histone-lysine N-methyltransferase SETD2 (SETD2) is a 2564-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BYW2.

Gene
SETD2
Organism
Homo sapiens
Length
2564 residues
Mean pLDDT
43.3
Model
AF-Q9BYW2-F1 v6
Model created
1 Aug 2025
PDB structures
43

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Model confidence (pLDDT)

The mean pLDDT of this model is 43.3 (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 accurate12%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions78%

What pLDDT means and how to read it

Function

Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate (PubMed:16118227, PubMed:19141475, PubMed:21526191, PubMed:21792193, PubMed:23043551, PubMed:27474439). It is capable of trimethylating unmethylated H3K36 (H3K36me0) in vitro (PubMed:19332550). Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation (By similarity). Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A (PubMed:23325844). Acts as a key regulator of DNA mismatch repair in G1…

Subunit structure

Specifically interacts with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A): binds to CTD heptad repeats doubly phosphorylated on 'Ser-2' and 'Ser-5' of each heptad (PubMed:16118227, PubMed:16314571). Interacts with HTT (PubMed:10958656, PubMed:11461154, PubMed:9700202). Interacts with IWS1 (PubMed:19141475). Interacts with p53/TP53; leading to regulate…

Subcellular location

Nucleus, Chromosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5JLBX-ray1.5 ÅA=1434-1711
5LT7X-ray1.51 ÅA=1433-1711
5LT8X-ray1.57 ÅA=1433-1711
7EVSX-ray1.6 ÅC/D=2180-2192
5LSYX-ray1.62 ÅA=1433-1711
5LSZX-ray1.62 ÅA=1433-1711
9G4AX-ray1.65 ÅA=1433-1711
6J9JX-ray1.78 ÅA=1447-1703
5LSSX-ray1.79 ÅA=1433-1711
7EVRX-ray1.8 ÅB/D=2167-2192
7LZDX-ray1.8 ÅA=1434-1711
8Q5PX-ray1.81 ÅA=1433-1711
9HGGX-ray1.9 ÅB=1363-1379
4H12X-ray1.99 ÅA=1434-1711
5JJYX-ray2.05 ÅA=1434-1711
5LT6X-ray2.05 ÅA/B=1433-1711
4FMUX-ray2.1 ÅA=1434-1711
8RZUX-ray2.19 ÅA=1433-1711
7LZBX-ray2.28 ÅA=1434-1711
6VDBX-ray2.3 ÅA=1433-1711

Showing 20 of 43 experimental structures (best resolution first).

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