P22579: Transcriptional regulatory protein SIN3 (SIN3)

Transcriptional regulatory protein SIN3 (SIN3) is a 1536-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P22579.

Gene
SIN3
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
1536 residues
Mean pLDDT
62.4
Model
AF-P22579-F1 v6
Model created
1 Aug 2025
PDB structures
27

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.4 (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 accurate17%
70 to 90Confident: backbone generally right33%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions39%

What pLDDT means and how to read it

Function

Catalytic component of the RPD3 histone deacetylase complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SIN3 also has a RPD3 independent function required for normal longevity

Subunit structure

Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6. Component of the RPD3C(S) complex composed of at least EAF3, RCO1, RPD3, SIN3, and UME1. Interacts with ESS1 and STB1

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6XAWX-ray1.84 ÅA=402-473
6XDJX-ray2.2 ÅA/B/C/D=402-473
8HPOEM2.6 ÅA/B=1-1536
8TOFEM2.8 ÅA=1-1536
8KD3EM2.9 ÅB=2-1536
8KD5EM2.9 ÅB=2-1536
8KD4EM2.93 ÅB=215-1536
8HXXEM3.0 ÅK=1-1536
8KD2EM3.02 ÅB=2-1536
8KD6EM3.07 ÅB=215-1536
8KD7EM3.09 ÅB=215-1536
8HXYEM3.1 ÅK=1-1536
8HY0EM3.1 ÅK=1-1536
7YI0EM3.2 ÅA=1-1536
7YI3EM3.3 ÅA=1-1536
8W9CEM3.3 ÅA=1-1536
8IHNEM3.37 ÅK=1-1536
7YI2EM3.4 ÅA=1-1536
8KC7EM3.46 ÅB=215-1536
8GA8EM3.5 ÅA/D=1-1536

Showing 20 of 27 experimental structures (best resolution first).

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