Sandbox 171
| 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. |
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| 2mys, resolution 2.80Å () | |||||||||
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| Ligands: | , | ||||||||
| Non-Standard Residues: | |||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
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] Each heavy chains composes the bulk of one of the globular heads. [1] Subfragment-1(S1) also termed the myosin head consists of ATP, actin, and two light chain binding sites.[1] Each globular head has a heavy chain and two light chains for a combined molecular size of about 130 kD. [1]
