2ppo Summary


Crystal structure of E60A mutant of FKBP12

The structure was published by Szep, S., Park, S., Boder, E.T., Van Duyne, G.D., and Saven, J.G., in 2009 in a paper entitled "Structural coupling between FKBP12 and buried water." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.29 Å and deposited in 2007.

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

The PDB entry contains the structure of FK506-binding protein 1A. 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.

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 1A 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 1A Homo sapiens

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

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

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