Evaluation of Synthetic FK506 Analogs as Ligands for the FK506-Binding Proteins 51 and 52: Complex of FKBP51 with 2-(3-((R)-3-(3,4-dimethoxyphenyl)-1-((S)-1-(2-((1R,2S)-2-ethyl-1-hydroxy-cyclohexyl)-2-oxoacetyl)piperidine-2-carbonyloxy)propyl)phenoxy)acetic acid from cocrystallization
The structure was published by Gopalakrishnan, R., Kozany, C., Gaali, S., et al., Hoogeland, B., Bracher, A., and Hausch, F., in 2012 in a paper entitled "Evaluation of Synthetic FK506 Analogues as Ligands for the FK506-Binding Proteins 51 and 52." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2012.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Peptidyl-prolyl cis-trans isomerase FKBP5. This molecule has the UniProt identifier Q13451 (FKBP5_HUMAN). The sample contained 128 residues which is < 90% of the natural sequence. Out of 128 residues 128 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 is most likely monomeric.
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: