X-ray structure of ERalpha LBD bound to a tetrahydroisoquinoline SERM ligand at 2.05A resolution
The structure was published by Renaud, J., Bischoff, S.F., Buhl, T., et al., Kallen, J., Keller, H.J., and Ramage, P., in 2005 in a paper entitled "Selective Estrogen Receptor Modulators with Conformationally Restricted Side Chains. Synthesis and Structure-Activity Relationship of ERalpha-Selective Tetrahydroisoquinoline Ligands" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.05 Å and deposited in 2004.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Estrogen 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: