SCALLOP MYOSIN S1-AMPPNP IN THE ACTIN-DETACHED CONFORMATION
The structure was published by Himmel, D.M., Gourinath, S., Reshetnikova, L., Shen, Y., Szent-Gyorgyi, A.G., and Cohen, C., in 2002 in a paper entitled "Crystallographic findings on the internally uncoupled and near-rigor states of myosin: Further insights into the mechanics of the motor" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 2002.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 3 biomacromolecules, namely MYOSIN heavy chain, MYOSIN REGULATORY LIGHT CHAIN, and MYOSIN ESSENTIAL LIGHT CHAIN.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule most likely forms heterotrimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 3 unique UniProt proteins: