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

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