Sandbox 171

Myosin is one of three major classes of molecular motors: myosin, dynein, and kinesin. As the most abundant of these proteins myosin plays a structural and enzymatic role in muscle contraction and intracellular motility.

Structure

Myosin has a molecular size of approximately 520 kilodaltons, with two 220 kD heavy chains and two pairs of light chains which vary in size. The molecule is asymmetric, having a long tail and two globular heads. The heavy chains each constitute a globular head.

Function

Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell.

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D load='2mys' size='350' frame='false' scene=
2mys, resolution 2.80Å (default scene)
Ligands:	MG, SO4
Non-Standard Residues:	MLY
Structural annotation: Resources: InterPro : Ipr001609, Ipr015650, Ipr002928, Ipr000048, Ipr004009 Pfam : PF00063, PF02736, PF00612 SCOP : d2mysa2, d2mysa1 UniProt : P13538, P02609, P02604
Functional annotation: Cellular component: myosin complex striated muscle thick filament Biological process: striated muscle contraction Molecular function: ATP binding actin binding calmodulin binding motor activity nucleotide binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml