O14497: AT-rich interactive domain-containing protein 1A (ARID1A)

AT-rich interactive domain-containing protein 1A (ARID1A) is a 2285-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O14497.

Gene
ARID1A
Organism
Homo sapiens
Length
2285 residues
Mean pLDDT
46.9
Model
AF-O14497-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 46.9 (very 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 accurate16%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions74%

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. Binds DNA non-specifically. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their…

Subunit structure

Component of SWI/SNF chromatin remodeling complexes, in some of which it can be mutually exclusive with ARID1B/BAF250B. 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 permitting…

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
6LTHEM3.0 ÅL=1-2285
9RL4EM3.5 ÅL=1-2285
6LTJEM3.7 ÅL=991-2285
9RN2EM4.1 ÅL=1-2285
9RMCEM4.2 ÅL=1-2285
9RN1EM5.9 ÅL=1-2285
1RYUNMRA=1000-1119

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