O75182: Paired amphipathic helix protein Sin3b (SIN3B)

Paired amphipathic helix protein Sin3b (SIN3B) is a 1162-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75182.

Gene
SIN3B
Organism
Homo sapiens
Length
1162 residues
Mean pLDDT
68.0
Model
AF-O75182-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.0 (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 accurate23%
70 to 90Confident: backbone generally right34%
50 to 70Low: treat with caution16%
Below 50Very low: often disordered regions27%

What pLDDT means and how to read it

Function

Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription. With FOXK1, regulates cell cycle progression probably by repressing cell cycle inhibitor genes expression. As part of the SIN3B complex represses transcription and counteracts the histone acetyltransferase activity of EP300 through the recognition H3K27ac marks by PHF12 and the activity of the histone deacetylase HDAC2 (PubMed:37137925). SIN3B complex is recruited downstream…

Subunit structure

Component of the SIN3B complex, which includes SIN3B, HDAC2 or HDAC1, PHF12 and MORF4L1 (PubMed:21041482, PubMed:37137925). Interacts with FOXK1/MNF, MXI, MAD, NCOR1 and SAP30. Interaction with SUDS3 enhances the interaction with HDAC1 to form a complex. Interacts with CRY1, HCFC1, MAD3, MAD4, MAEL, REST, RNF220 and SETDB1. Interacts with C6orf89 (PubMed:23460338). Interacts with MYT1L (By…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8BPBEM2.8 ÅA=1-1162
8BPCEM2.8 ÅA=1-1162
8C60EM3.4 ÅA=1-1162
8BPAEM3.7 ÅA=1-1162

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