Fk1 domain mutant A19T of FKBP51, crystal form IV, in presence of DMSO
The structure was published by Bracher, A., Kozany, C., Thost, A.K., and Hausch, F., in 2011 in a paper entitled "Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 0.96 Å and deposited in 2010.
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 126 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: