Q9QZZ4: Unconventional myosin-XV (Myo15a)

Unconventional myosin-XV (Myo15a) is a 2306-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9QZZ4.

Gene
Myo15a
Organism
Mus musculus
Length
2306 residues
Mean pLDDT
70.7
Model
AF-Q9QZZ4-3-F1 v6
Model created
1 Aug 2025
PDB structures
7

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 70.7 (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 accurate12%
70 to 90Confident: backbone generally right57%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions23%

What pLDDT means and how to read it

Function

Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). Required for the arrangement of stereocilia in mature hair bundles

Subunit structure

Interacts with the third PDZ domain of WHRN which is necessary for localization of WHRN to stereocilium tips. Interacts with FASLG (By similarity). Interacts with EPS8

Subcellular location

Cell projection, stereocilium, Cytoplasm, cytoskeleton

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6Y38X-ray1.7 ÅC/D=3499-3511
6Y9NX-ray1.93 ÅB=3499-3511
7R91EM2.83 ÅD=1205-1889
7UDTEM3.17 ÅD=1205-1923
7RB8EM3.63 ÅD=1205-1889
7RB9EM3.76 ÅD=1205-1889
7UDUEM4.15 ÅD=1205-1923

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.