P80428: Actin-related protein 4 (ARP4)

Actin-related protein 4 (ARP4) is a 489-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P80428.

Gene
ARP4
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
489 residues
Mean pLDDT
85.3
Model
AF-P80428-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.3 (confident 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 accurate76%
70 to 90Confident: backbone generally right7%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Chromatin interaction component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. ARP4 recognizes H2AS128ph (gamma-H2A) and is required for NuA4 complex integrity. Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the INO80 complex which remodels chromatin by shifting nucleosomes. Its ability to induce transcription of some phosphate-responsive genes is modulated by…

Subunit structure

Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, SWC4, TRA1, VID21, YAF9 and YNG2. Component of the chromatin-remodeling INO80 complex, at least composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80. Component of the SWR1 chromatin remodeling complex composed of at…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5I9EX-ray2.8 ÅA/C=1-489
5NBLX-ray2.8 ÅA/B=1-489
7VVYEM3.1 ÅF=1-489
8ESCEM3.1 ÅR=1-489
8A5OEM3.2 ÅW=1-489
8A5AEM3.3 ÅW=1-489
3QB0X-ray3.4 ÅA/B/C/D=1-489
5NBMX-ray3.4 ÅA/B=1-489
7YFNEM3.8 ÅB=1-489
5NBNX-ray4.0 ÅA/B=1-489
7YFPEM4.0 ÅB=8-488
5Y81EM4.7 ÅF=1-489
7VVZEM8.8 ÅF=1-489

More AlphaFold highlights

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