P13538: Myosin heavy chain, skeletal muscle, adult

Myosin heavy chain, skeletal muscle, adult is a 1939-residue protein from Gallus gallus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P13538.

Organism
Gallus gallus
Length
1939 residues
Mean pLDDT
74.6
Model
AF-P13538-F1 v6
Model created
1 Aug 2025
PDB structures
15

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 74.6 (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 accurate11%
70 to 90Confident: backbone generally right55%
50 to 70Low: treat with caution31%
Below 50Very low: often disordered regions4%

What pLDDT means and how to read it

Function

Muscle contraction. Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin

Subunit structure

Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2)

Subcellular location

Cytoplasm, myofibril

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2MYSX-ray2.8 ÅA=2-844
2W4AEM35.0 ÅM=5-844
2W4GEM35.0 ÅM=5-844
2W4HEM35.0 ÅM=5-844
1M8QEM70.0 ÅA/D/G/P=5-844
1MVWEM70.0 ÅA/D/G/J/M/P=5-844
1O18EM70.0 ÅA/D/G/J/M/P=5-844
1O19EM70.0 ÅA/D/G/J/M/S=5-844
1O1AEM70.0 ÅA/D/G/J/M/P=5-844
1O1BEM70.0 ÅA/D/G/J=5-844
1O1CEM70.0 ÅA/D/G/J/P=5-844
1O1DEM70.0 ÅA/D/G/J/M/P=5-844
1O1EEM70.0 ÅA/D/G/J/M/P=5-844
1O1FEM70.0 ÅA/D/G/J=5-844
1O1GEM70.0 ÅA/D/G/J/M/P=5-844

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.