Q15022: Polycomb protein SUZ12 (SUZ12)

Polycomb protein SUZ12 (SUZ12) is a 739-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15022.

Gene
SUZ12
Organism
Homo sapiens
Length
739 residues
Mean pLDDT
71.0
Model
AF-Q15022-F1 v6
Model created
1 Aug 2025
PDB structures
30

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Model confidence (pLDDT)

The mean pLDDT of this model is 71.0 (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 right24%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions31%

What pLDDT means and how to read it

Function

Polycomb group (PcG) protein. Component of the PRC2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene (PubMed:15225548, PubMed:15231737, PubMed:15385962, PubMed:16618801, PubMed:17344414, PubMed:18285464, PubMed:28229514, PubMed:29499137, PubMed:31959557). The PRC2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems (PubMed:12351676, PubMed:12435631, PubMed:15099518, PubMed:15225548, PubMed:15385962, PubMed:15684044, PubMed:16431907, PubMed:18086877, PubMed:18285464). Genes repressed by the PRC2 complex include HOXC8,…

Subunit structure

Component of the PRC2 complex, which consists of the core subunits EED, EZH1 or EZH2, SUZ12, and RBBP4, and various combinations of accessory subunits including AEBP2, JARID2, PHF19, MTF2 and EPOP (PubMed:12351676, PubMed:12435631, PubMed:15099518, PubMed:15225548, PubMed:15385962, PubMed:15684044, PubMed:16224021, PubMed:18285464, PubMed:19026781, PubMed:29499137, PubMed:31959557). Within the…

Subcellular location

Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5IJ7X-ray2.62 ÅS/T=545-725
9XZIX-ray2.69 ÅA=76-545
4W2RX-ray2.81 ÅS/T=545-725
6NQ3X-ray2.89 ÅB/F=76-545
5WAIX-ray2.9 ÅB/F=76-545
5HYNX-ray2.95 ÅC/H/M/S=558-685
5IJ8X-ray2.99 ÅS/T=545-725
7TD5X-ray2.99 ÅC/H=561-739
6B3WX-ray3.05 ÅS/T=545-725
8VMIEM3.1 ÅL/T=1-739
8VNVEM3.1 ÅA=68-685
9C8UEM3.1 ÅB=1-739
5WAKX-ray3.2 ÅB=76-545
8FYHEM3.4 ÅB/H=1-739
9DCHEM3.4 ÅB/I=1-739
5LS6X-ray3.47 ÅC/F/I/L=558-685
6C24EM3.5 ÅA/M/Q=1-739
6WKREM3.5 ÅA=1-739
8VMLEM3.5 ÅA=1-739
8VNZEM3.5 ÅA=1-739

Showing 20 of 30 experimental structures (best resolution first).

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