P51532: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin… (SMARCA4)

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin… (SMARCA4) is a 1647-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P51532.

Gene
SMARCA4
Organism
Homo sapiens
Length
1647 residues
Mean pLDDT
64.0
Model
AF-P51532-F1 v6
Model created
1 Aug 2025
PDB structures
28

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Model confidence (pLDDT)

The mean pLDDT of this model is 64.0 (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 accurate19%
70 to 90Confident: backbone generally right31%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions37%

What pLDDT means and how to read it

Function

ATPase 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:15075294, PubMed:29374058, PubMed:30339381, PubMed:32459350). Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating the calcium-dependent release of a repressor complex and the recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by…

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
7TABX-ray1.16 ÅA=1448-1575
2GRCX-ray1.5 ÅA=1448-1575
6ZS2X-ray1.57 ÅA/B=1451-1569
7TD9X-ray1.61 ÅAAA/BBB/CCC=1448-1575
6HR2X-ray1.76 ÅA/E=1449-1568
3UVDX-ray1.85 ÅA=1448-1569
5DKDX-ray2.0 ÅA/B=1451-1569
5EA1X-ray2.0 ÅA/B/C=1451-1580
9DTXX-ray2.11 ÅD=1448-1569
7VRBX-ray2.39 ÅA/B/C/D=172-213
7VDTEM2.8 ÅA=160-1647
9WBZEM2.9 ÅA=1-1647
6LTHEM3.0 ÅI=1-1647
9UX9EM3.05 ÅK=2-1647
8QJRX-ray3.17 ÅG/H=1451-1569
7VDVEM3.4 ÅA=160-1647
9WC1EM3.4 ÅD=1-1647
9RL4EM3.5 ÅI=1-1647
6LTJEM3.7 ÅI=1-1647
8G1QX-ray3.73 ÅH=1447-1569

Showing 20 of 28 experimental structures (best resolution first).

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