3ey6 Summary

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Crystal structure of the FK506-binding domain of human FKBP38

The structure was published by Maestre-Martinez, M., Haupt, K., Edlich, F., et al., Stubbs, M.T., Fischer, G., and Luecke, C., in 2011 in a paper entitled "A charge-sensitive loop in the FKBP38 catalytic domain modulates Bcl-2 binding." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.05 Å and deposited in 2008.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of FK506-binding protein 8. This molecule has the UniProt identifier Q14318 (FKBP8_HUMAN)search. The sample contained 121 residues which is < 90% of the natural sequence. Out of 121 residues 118 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 FK506-binding protein 8 Q14318 (92-210) (FKBP8_HUMAN)search Homo sapienssearch < 90% 121 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q14318 (92 - 210) FK506-binding protein 8 Homo sapiens

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

Chain ID Biological process (GO)
A (Q14318) protein foldingsearch

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