HUMAN OESTROGEN RECEPTOR BETA LIGAND-BINDING DOMAIN IN COMPLEX WITH PARTIAL AGONIST GENISTEIN
The structure was published by Pike, A.C.W., Brzozowski, A.M., Hubbard, R.E., et al., Ljunggren, J., Gustaffson, J.-A., and Carlquist, M., in 1999 in a paper entitled "Structure of the Ligand-Binding Domain of Oestrogen Receptor Beta in the Presence of a Partial Agonist and a Full Antagonist" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of ESTROGEN RECEPTOR BETA. This molecule has the UniProt identifier Q92731 (ESR2_HUMAN). The sample contained 255 residues which is < 90% of the natural sequence. Out of 255 residues 226 were observed and are deposited in the PDB.
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 homodimers.
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: