The Ligandable Human Proteome

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FKBP-type peptidyl-prolyl cis-trans isomerase domain

IndexGene Name PrimaryProtein NameUniprot IDGene Name SynonymLigand NameStructurePDB Codeligand desolvationLigand StructureCompound Affinity nM
1FKB1APeptidyl-prolyl cis-trans isomerase FKBP1AP62942FKBP1 FKBP12tstcrystal structure analysis of the FKBP12 complexed with 000308 small molecule1j4i71.14no data
2FKB1APeptidyl-prolyl cis-trans isomerase FKBP1AP62942FKBP1 FKBP12sbxDESIGN, SYNTHESIS, AND KINETIC EVALUATION OF HIGH-AFFINITY FKBP LIGANDS, AND THE X-RAY CRYSTAL STRUCTURES OF THEIR COMPLEXES WITH FKBP121fkh65.447.
3FKB1APeptidyl-prolyl cis-trans isomerase FKBP1AP62942FKBP1 FKBP12sb3DESIGN, SYNTHESIS, AND KINETIC EVALUATION OF HIGH-AFFINITY FKBP LIGANDS, AND THE X-RAY CRYSTAL STRUCTURES OF THEIR COMPLEXES WITH FKBP121fkg65.5910.
4FKBP4Peptidyl-prolyl cis-trans isomerase FKBP4Q02790FKBP52i63Crystal Structure Analysis of FKBP52, Complex with I634lay61.91no data
5FKBP5Peptidyl-prolyl cis-trans isomerase FKBP5Q13451AIG6 FKBP51jfkIncreasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by Conformational Control: Complex of FKBP51 with (1S,6R)-3-[2-(3,4-dimethoxyphenoxy)ethyl]-10-[(2-oxo-2,3-dihydro-1,3-benzothiazol-6-yl)sulfonyl]-3,10-diazabicyclo[4.3.1]decan-2-one4jfk69.26360.
6FKBP5Peptidyl-prolyl cis-trans isomerase FKBP5Q13451AIG6 FKBP51i63EVALUATION OF SYNTHETIC FK506 ANALOGS AS LIGANDS FOR FKBP51 AND FKBP52: COMPLEX OF FKBP51 WITH {3-[(1R)-3-(3,4-dimethoxyphenyl)-1-({[(2S)-1-(3,3-dimethyl-2-oxopentanoyl)piperidin-2-yl]carbonyl}oxy)propyl]phenoxy}acetic acid4drk59.278360.
7FKBP5Peptidyl-prolyl cis-trans isomerase FKBP5Q13451AIG6 FKBP515bhThe Fk1 domain of FKBP51 in complex with the new synthetic ligand (S)-N-(1-carbamoylcyclopentyl)-1-((S)-2-cyclohexyl-2-(3,4,5-trimethoxyphenyl)acetyl)piperidine-2-carboxamide5div73.16140.
8FKBP5Peptidyl-prolyl cis-trans isomerase FKBP5Q13451AIG6 FKBP513jpThe Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-[(3,5-dichlorophenyl)sulfonyl]-3-[2-(3,4-dimethoxyphenoxy)ethyl]-5-ethyl-3,10-diazabicyclo[4.3.1]decan-2-one4w9q65.78140.
9FKBP5Peptidyl-prolyl cis-trans isomerase FKBP5Q13451AIG6 FKBP511kzIncreasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by Conformational Control: Complex of FKBP51 with 2-(3,4-dimethoxyphenoxy)ethyl (2S)-1-[(2-oxo-2,3-dihydro-1,3-benzothiazol-6-yl)sulfonyl]piperidine-2-carboxylate4jfm64.113300.
10FKBP5Peptidyl-prolyl cis-trans isomerase FKBP5Q13451AIG6 FKBP511kyIncreasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by Conformational Control: Complex of FKBP51 with 6-({(1S,5R)-3-[2-(3,4-dimethoxyphenoxy)ethyl]-2-oxo-3,9-diazabicyclo[3.3.1]non-9-yl}sulfonyl)-1,3-benzothiazol-2(3H)-one4jfl66.4610500.
11FKBP5Peptidyl-prolyl cis-trans isomerase FKBP5Q13451AIG6 FKBP511kuIncreasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by Conformational Control: Complex of FKBP51 with compound (1S,6R)-10-(1,3-benzothiazol-6-ylsulfonyl)-3-[2-(3,4-dimethoxyphenoxy)ethyl]-3,10-diazabicyclo[4.3.1]decan-2-one4jfj66.632100.
12FKBP5Peptidyl-prolyl cis-trans isomerase FKBP5Q13451AIG6 FKBP511ktIncreasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by Conformational Control: Complex of FKBP51 with compound 1-[(9S,13R,13aR)-1,3-dimethoxy-8-oxo-5,8,9,10,11,12,13,13a-octahydro-6H-9,13-epiminoazocino[2,1-a]isoquinolin-14-yl]-2-(3,4,5-trimethoxyphenyl)ethane-1,2-dione4jfi70.3818100.
13FKBP5Peptidyl-prolyl cis-trans isomerase FKBP5Q13451AIG6 FKBP51384The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-[(3,5-dichlorophenyl)sulfonyl]-5-(2-methoxyethoxy)-3-(2-methoxyethyl)-3,10-diazabicyclo[4.3.1]decan-2-one4tx068.59no data
14FKBP5Peptidyl-prolyl cis-trans isomerase FKBP5Q13451AIG6 FKBP519qnThe Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-((3,5-dichlorophenyl)sulfonyl)-5-(hydroxymethyl)-3-(pyridin-2-ylmethyl)-3,10-diazabicyclo[4.3.1]decan-2-one5obk67.15no data