3o5q Summary


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)search. 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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Peptidyl-prolyl cis-trans isomerase FKBP5 Q13451 (16-140) (FKBP5_HUMAN)search Homo sapienssearch 100% 128 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q13451 (16 - 140) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens

Chain Sequence family (Pfam)
A (Q13451) PF00254: FKBP-type peptidyl-prolyl cis-trans isomerasesearch

Chain ID Biological process (GO)
A (Q13451) protein foldingsearch

Chain InterPro annotation
A Peptidyl-prolyl cis-trans isomerase, FKBP-type, domainsearch Peptidyl-prolyl cis-trans isomerase, FKBP-typesearch