O96019: Actin-like protein 6A (ACTL6A)

Actin-like protein 6A (ACTL6A) is a 429-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O96019.

Gene
ACTL6A
Organism
Homo sapiens
Length
429 residues
Mean pLDDT
91.6
Model
AF-O96019-F1 v6
Model created
1 Aug 2025
PDB structures
21

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Model confidence (pLDDT)

The mean pLDDT of this model is 91.6 (very high 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 accurate87%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions4%

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. Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch…

Subunit structure

Component of numerous complexes with chromatin remodeling and histone acetyltransferase activity. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8QR1EM2.4 ÅK=1-429
9C57EM2.75 ÅL/M=1-429
9WBZEM2.9 ÅN=1-429
9CAEEM3.07 ÅM=1-429
8X15EM3.2 ÅT=1-429
8X19EM3.2 ÅT=1-429
8X1CEM3.2 ÅT=1-429
8XVTEM3.2 ÅI/J=1-429
9C6NEM3.29 ÅL=1-429
7VDVEM3.4 ÅN=1-429
9C4BEM3.4 ÅA=1-429
9WC1EM3.4 ÅB=1-429
9CACEM3.43 ÅM=1-429
9RL4EM3.5 ÅJ=1-429
6LTJEM3.7 ÅJ=12-417
9RN2EM4.1 ÅJ=1-429
9RMCEM4.2 ÅJ=1-429
7Y8REM4.4 ÅK=1-429
9C62EM5.28 ÅL/M=1-429
9RN1EM5.9 ÅJ=1-429

Showing 20 of 21 experimental structures (best resolution first).

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