Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
The structure was published by English, C.M., Adkins, M.W., Carson, J.J., Churchill, M.E., and Tyler, J.K., in 2006 in a paper entitled "Structural basis for the histone chaperone activity of asf1." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2006.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 3 biomacromolecules, namely Anti-silencing protein 1, Histone H3, and Histone H4.
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 has more than one probable quaternary state observed. For more details see the quaternary structure page.
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: