P61158: Actin-related protein 3 (ACTR3)

Actin-related protein 3 (ACTR3) is a 418-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61158.

Gene
ACTR3
Organism
Homo sapiens
Length
418 residues
Mean pLDDT
91.3
Model
AF-P61158-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 91.3 (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 accurate81%
70 to 90Confident: backbone generally right12%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9000076). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9000076). Seems to contact the pointed end of the daughter actin filament (PubMed:9000076). In podocytes, required for the formation of lamellipodia downstream of AVIL and PLCE1 regulation (PubMed:29058690). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of…

Subunit structure

Component of the Arp2/3 complex composed of ACTR2/ARP2, ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC (PubMed:11741539, PubMed:9000076, PubMed:9230079). Interacts with WHDC1 (PubMed:18614018). Interacts weakly with MEFV (PubMed:19109554). Interacts with AVIL (PubMed:29058690)

Subcellular location

Cytoplasm, cytoskeleton, Cell projection, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9I2BEM3.0 ÅA/K=1-418
8P94EM3.3 ÅA=1-418
6UHCEM3.9 ÅA=1-418
6YW6EM4.2 ÅA=1-418
6YW7EM4.5 ÅA=1-418

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