3o5g Summary


Fk1 domain of FKBP51, crystal form I

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 2.0 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 127 were observed and are deposited in the PDB.

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