Q2M3X8: Phosphatase and actin regulator 1 (Phactr1)

Phosphatase and actin regulator 1 (Phactr1) is a 580-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q2M3X8.

Gene
Phactr1
Organism
Mus musculus
Length
580 residues
Mean pLDDT
62.5
Model
AF-Q2M3X8-F1 v6
Model created
1 Aug 2025
PDB structures
6

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 62.5 (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 accurate21%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution17%
Below 50Very low: often disordered regions45%

What pLDDT means and how to read it

Function

Binds actin monomers (G actin) and plays a role in multiple processes including the regulation of actin cytoskeleton dynamics, actin stress fibers formation, cell motility and survival, formation of tubules by endothelial cells, and regulation of PPP1CA activity. Involved in the regulation of cortical neuron migration and dendrite arborization (PubMed:30256902)

Subunit structure

Interacts (via RPEL repeats) with ACTA1 and PPP1CA; ACTA1 and PPP1CA compete for the same binding site

Subcellular location

Cytoplasm, Synapse, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4B1YX-ray1.29 ÅM=493-524
4B1VX-ray1.75 ÅM/N=133-164
4B1XX-ray1.8 ÅM=455-486
4B1WX-ray1.95 ÅM=417-448
4B1UX-ray2.0 ÅM=133-164
4B1ZX-ray3.3 ÅM/N=414-528

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.