Q5T6S3: PHD finger protein 19 (PHF19)

PHD finger protein 19 (PHF19) is a 580-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q5T6S3.

Gene
PHF19
Organism
Homo sapiens
Length
580 residues
Mean pLDDT
69.1
Model
AF-Q5T6S3-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 69.1 (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 accurate44%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions37%

What pLDDT means and how to read it

Function

Polycomb group (PcG) protein that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex, thus enhancing PRC2 H3K27me3 methylation activity (PubMed:15563832, PubMed:18691976, PubMed:23104054, PubMed:23160351, PubMed:23228662, PubMed:23273982, PubMed:29499137, PubMed:31959557). Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting H3K36me3 histone demethylases RIOX1 or KDM2B, leading to demethylation of H3K36 and recruitment of the PRC2 complex that mediates H3K27me3 methylation, followed by de novo silencing…

Subunit structure

Associates with the PRC2 complex, which consists of the core components EED, EZH1 or EZH2, SUZ12, and RBBP4, and various combinations of accessory subunits including AEBP2, JARID2, PHF19, MTF2 and EPOP (PubMed:23104054, PubMed:29499137, PubMed:31959557). Forms a dimeric PRC2.1 (class 1, PRC-PCL) complex consisting of at least SUZ12, RBBP4, and PHF19 or MTF2; PHF19 and MTF2 stabilize the dimeric…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6WAUX-ray1.75 ÅA/B/C/D/E/F=38-96
9XZIX-ray2.69 ÅC=531-580
6NQ3X-ray2.89 ÅC/G=500-580
2E5QNMRA=40-95
4BD3NMRA=38-95

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