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.

StructureStructure

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. ^[1] The molecule is asymmetric, having a long tail and two globular heads. ^[1] The heavy chains each constitute a globular head. ^[1]

FunctionFunction

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.

2mys, resolution 2.80Å ()

Ligands:

,

Non-Standard Residues:

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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Andrea Gorrell, Laurel Koopmans

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