1fkd Summary

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FK-506 BINDING PROTEIN: THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX WITH THE ANTAGONIST L-685,818

The structure was published by Becker, J.W., Rotonda, J., McKeever, B.M., et al., Wiederrecht, G., Hermes, J.D., and Springer, J.P., in 1993 in a paper entitled "FK-506-binding protein: three-dimensional structure of the complex with the antagonist L-685,818." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.72 Å and deposited in 1992.

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

The PDB entry contains the structure of FK506 BINDING PROTEIN. This molecule has the UniProt identifier P62942 (FKB1A_HUMAN)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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 P62942 (2-108) (FKB1A_HUMAN)search Homo sapienssearch 99% 107 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P62942 (2 - 108) FK506 BINDING PROTEIN Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P62942) FKBP immunophilin/proline isomerasesearch Chitinase A; domain 3search PF00254: FKBP-type peptidyl-prolyl cis-trans isomerasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P62942) protein bindingsearch FK506 bindingsearch SMAD bindingsearch peptidyl-prolyl cis-trans isomerase activitysearch ion channel bindingsearch type I transforming growth factor beta receptor bindingsearch isomerase activitysearch transforming growth factor beta receptor bindingsearch signal transducer activitysearch calcium channel inhibitor activitysearch macrolide bindingsearch activin bindingsearch calcium ion transmembrane transportsearch transforming growth factor beta receptor signaling pathwaysearch positive regulation of protein bindingsearch T cell activationsearch amyloid fibril formationsearch heart morphogenesissearch 'de novo' protein foldingsearch chaperone-mediated protein foldingsearch SMAD protein complex assemblysearch positive regulation of protein ubiquitinationsearch regulation of immune responsesearch protein peptidyl-prolyl isomerizationsearch protein maturation by protein foldingsearch regulation of amyloid precursor protein catabolic processsearch protein refoldingsearch negative regulation of release of sequestered calcium ion into cytosolsearch protein foldingsearch negative regulation of ryanodine-sensitive calcium-release channel activitysearch positive regulation of I-kappaB kinase/NF-kappaB signalingsearch ventricular cardiac muscle tissue morphogenesissearch regulation of ryanodine-sensitive calcium-release channel activitysearch heart trabecula formationsearch regulation of protein localizationsearch extracellular fibril organizationsearch regulation of activin receptor signaling pathwaysearch negative regulation of protein phosphatase type 2B activitysearch cytosolsearch extracellular vesicular exosomesearch cytoplasmsearch terminal cisternasearch Z discsearch membranesearch endoplasmic reticulum membranesearch

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