P35579: Myosin-9 (MYH9)

Myosin-9 (MYH9) is a 1960-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P35579.

Gene
MYH9
Organism
Homo sapiens
Length
1960 residues
Mean pLDDT
76.2
Model
AF-P35579-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 76.2 (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 accurate16%
70 to 90Confident: backbone generally right55%
50 to 70Low: treat with caution25%
Below 50Very low: often disordered regions4%

What pLDDT means and how to read it

Function

Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Required for cortical actin clearance prior to oocyte exocytosis (By similarity). Promotes cell motility in conjunction with S100A4 (PubMed:16707441). During cell spreading, plays an important role in cytoskeleton reorganization, focal contact formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 (PubMed:20052411)

Subunit structure

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). Interacts with RASIP1 (By similarity). Interacts with DDR1 (By similarity). Interacts with PDLIM2 (By similarity). Interacts with SVIL (PubMed:12917436, PubMed:17925381). Interacts with HTRA3 (PubMed:22229724). Interacts with Myo7a (By…

Subcellular location

Cytoplasm, cytoskeleton, Cytoplasm, cell cortex, Cytoplasmic vesicle, secretory vesicle, Cortical granule, Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4CFQX-ray1.37 ÅQ/R=1893-1937
4CFRX-ray1.4 ÅQ=1893-1937
4ETOX-ray1.54 ÅP=1908-1923
3ZWHX-ray1.94 ÅQ=1893-1937
9IHLX-ray2.02 ÅA=1-775
9SYUEM2.98 ÅA/B/G/H=1-1960
9SZREM6.3 ÅA/B=1-1960
2LNKNMRC=1897-1935

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