1f40 Summary



The structure was published by Sich, C., Improta, S., Cowley, D.J., et al., Merly, J.P., Teufel, M., and Saudek, V., in 2000 in a paper entitled "Solution structure of a neurotrophic ligand bound to FKBP12 and its effects on protein dynamics." (abstract).

The structure was determined using NMR spectroscopy and deposited in 2000.

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

The PDB entry contains the structure of FK506 BINDING PROTEIN (FKBP12). 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 FK506 BINDING PROTEIN (FKBP12) 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 (FKBP12) 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 Cellular component (GO) Biological process (GO) Molecular function (GO)
A (P62942) cytoplasmsearch extracellular vesicular exosomesearch cytosolsearch terminal cisternasearch Z discsearch membranesearch endoplasmic reticulum membranesearch positive regulation of protein bindingsearch regulation of immune responsesearch extracellular fibril organizationsearch protein foldingsearch protein maturation by protein foldingsearch ventricular cardiac muscle tissue morphogenesissearch transforming growth factor beta receptor signaling pathwaysearch 'de novo' protein foldingsearch regulation of activin receptor signaling pathwaysearch SMAD protein complex assemblysearch negative regulation of protein phosphatase type 2B activitysearch T cell activationsearch positive regulation of I-kappaB kinase/NF-kappaB signalingsearch heart morphogenesissearch regulation of amyloid precursor protein catabolic processsearch chaperone-mediated protein foldingsearch protein peptidyl-prolyl isomerizationsearch negative regulation of release of sequestered calcium ion into cytosolsearch calcium ion transmembrane transportsearch protein refoldingsearch regulation of protein localizationsearch negative regulation of ryanodine-sensitive calcium-release channel activitysearch regulation of ryanodine-sensitive calcium-release channel activitysearch positive regulation of protein ubiquitinationsearch heart trabecula formationsearch amyloid fibril formationsearch protein bindingsearch transforming growth factor beta-activated receptor activitysearch transforming growth factor beta receptor bindingsearch activin bindingsearch peptidyl-prolyl cis-trans isomerase activitysearch ryanodine-sensitive calcium-release channel activitysearch FK506 bindingsearch signal transducer activitysearch ion channel bindingsearch SMAD bindingsearch isomerase activitysearch type I transforming growth factor beta receptor bindingsearch macrolide bindingsearch calcium channel inhibitor activitysearch

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