4dh0 Summary

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X-ray Crystal Structure of 28-O-Methylrapamycin complexed with FKBP12: Is the Cyclohexyl Moiety Part of the Effector Domain of Rapamycin?

The structure was published by Kallen, J., Sedrani, R., and Cottens, S., in 1996 in a paper entitled "X-ray Crystal Structure of 28-O-Methylrapamycin complexed with FKBP12: Is the Cyclohexyl Moiety Part of the Effector Domain of Rapamycin?" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2012.

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

The PDB entry contains the structure of Peptidyl-prolyl cis-trans isomerase FKBP1A. 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 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 Peptidyl-prolyl cis-trans isomerase FKBP1A 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) Peptidyl-prolyl cis-trans isomerase FKBP1A Homo sapiens

Chain Sequence family (Pfam)
A (P62942) PF00254: FKBP-type peptidyl-prolyl cis-trans isomerasesearch

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

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