1fkl Summary



The structure was published by Wilson, K.P., Yamashita, M.M., Sintchak, M.D., et al., Fitzgibbon, M.J., Black, J.R., and Navia, M.A., in 1995 in a paper entitled "Comparative X-ray structures of the major binding protein for the immunosuppressant FK506 (tacrolimus) in unliganded form and in complex with FK506 and rapamycin." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1995.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of FK506 BINDING PROTEIN. This molecule has the UniProt identifier P18203 (FKB1A_BOVIN)search. The sample contained 107 residues which is 99% of the natural sequence. Out of 107 residues 107 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 FK506 BINDING PROTEIN P18203 (2-108) (FKB1A_BOVIN)search Bos taurussearch 99% 107 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P18203 (2 - 108) FK506 BINDING PROTEIN Bos taurus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P18203) FKBP immunophilin/proline isomerasesearch Chitinase A; domain 3search PF00254: FKBP-type peptidyl-prolyl cis-trans isomerasesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P18203) protein peptidyl-prolyl isomerizationsearch ventricular cardiac muscle tissue morphogenesissearch protein foldingsearch muscle contractionsearch cytokine-mediated signaling pathwaysearch negative regulation of release of sequestered calcium ion into cytosolsearch negative regulation of protein phosphorylationsearch chaperone-mediated protein foldingsearch response to caffeinesearch release of sequestered calcium ion into cytosolsearch heart trabecula formationsearch T cell proliferationsearch T cell activationsearch regulation of ryanodine-sensitive calcium-release channel activitysearch heart morphogenesissearch FK506 bindingsearch protein homodimerization activitysearch ion channel bindingsearch drug bindingsearch calcium channel inhibitor activitysearch isomerase activitysearch peptidyl-prolyl cis-trans isomerase activitysearch endoplasmic reticulum membranesearch cytosolsearch membranesearch cytoplasmsearch sarcoplasmic reticulum membranesearch

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