Crystal structure of the human progesterone receptor ligand-binding domain bound to levonorgestrel
The structure was published by Petit-Topin, I., Turque, N., Fagart, J., et al., Ulmann, A., Gainer, E., and Rafestin-Oblin, M.E., in 2009 in a paper entitled "Met909 plays a key role in the activation of the progesterone receptor and also in the high potency of 13-ethyl progestins" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.26 Å and deposited in 2008.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Progesterone receptor.
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 1 unique UniProt protein: