Q8TAQ2: SWI/SNF complex subunit SMARCC2 (SMARCC2)

SWI/SNF complex subunit SMARCC2 (SMARCC2) is a 1214-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8TAQ2.

Gene
SMARCC2
Organism
Homo sapiens
Length
1214 residues
Mean pLDDT
63.4
Model
AF-Q8TAQ2-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.4 (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 accurate28%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions44%

What pLDDT means and how to read it

Function

Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (PubMed:11018012). Can stimulate the ATPase activity of the catalytic subunit of these complexes (PubMed:10078207). May be required for CoREST dependent repression of neuronal specific gene promoters in non-neuronal cells (PubMed:12192000). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific…

Subunit structure

Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present…

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
6KAGX-ray2.6 ÅB/C=325-518
6LTHEM3.0 ÅN/O=1-1214
7VDVEM3.4 ÅW/X=1-1214
9RL4EM3.5 ÅN/O=1-1214
6LTJEM3.7 ÅN/O=1-1214
9RN2EM4.1 ÅN/O=1-1214
9RMCEM4.2 ÅN/O=1-1214
7Y8REM4.4 ÅN/O=1-1214
9RN1EM5.9 ÅN/O=1-1214

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