1fkf Summary

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ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX

The structure was published by Van Duyne, G.D., Standaert, R.F., Karplus, P.A., Schreiber, S.L., and Clardy, J., in 1991 in a paper entitled "Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1991.

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 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 most likely forms homodimers.

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

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