Q02440: Unconventional myosin-Va (MYO5A)

Unconventional myosin-Va (MYO5A) is a 1829-residue protein from Gallus gallus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q02440.

Gene
MYO5A
Organism
Gallus gallus
Length
1829 residues
Mean pLDDT
77.3
Model
AF-Q02440-F1 v6
Model created
1 Aug 2025
PDB structures
31

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.3 (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 accurate28%
70 to 90Confident: backbone generally right48%
50 to 70Low: treat with caution14%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Can hydrolyze ATP in the presence of actin, which is essential for its function as a motor protein. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation

Subunit structure

May be a homodimer, which associates with multiple calmodulin or myosin light chains

Subcellular location

Golgi apparatus membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1W7JX-ray2.0 ÅA=1-792
1OE9X-ray2.05 ÅA=1-792
1W8JX-ray2.7 ÅA/B/C/D=1-766
7PMDEM2.9 ÅA=1-792
7PMEEM2.9 ÅA/D=1-792
1W7IX-ray3.0 ÅA=1-792
7PM6EM3.0 ÅA/D=1-792
7PM5EM3.1 ÅA=1-792
7PLUEM3.2 ÅA/D=1-792
7PLYEM3.2 ÅA=1-792
7PLZEM3.2 ÅA/D=1-792
7PLTEM3.3 ÅA=1-792
7PMGEM3.3 ÅA=1-792
7PMIEM3.3 ÅA=1-792
7PMLEM3.3 ÅA=1-792
7PMFEM3.4 ÅA=1-792
7PMHEM3.4 ÅA=1-792
7PMJEM3.4 ÅA=1-792
7PLVEM3.5 ÅA=1-792
7PLWEM3.5 ÅA=1-792

Showing 20 of 31 experimental structures (best resolution first).

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