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Structure paper

TitleStructure-Affinity Relationship Analysis of Selective FKBP51 Ligands.
Journal, issue, pagesJ. Med. Chem., Vol. 58, Page 7796-7806, Year 2015
Publish dateSep 1, 2015 (structure data deposition date)
AuthorsFeng, X. / Sippel, C. / Bracher, A. / Hausch, F.
External linksJ. Med. Chem. / PubMed:26419422
MethodsX-ray diffraction
Resolution2.25 Å
Structure data

PDB-5dit:
The Fk1 domain of FKBP51 in complex with the new synthetic ligand (1R)-3-(3,4-dimethoxyphenyl)-1-f3-[2-(morpholin-4-yl)ethoxy]phenylgpropyl(2S)-1-[(2S,3R)-2-cyclohexyl-3-hydroxybutanoyl]piperidine-2-carboxylate
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

Chemicals

ChemComp-5B8:
(1R)-3-(3,4-dimethoxyphenyl)-1-{3-[2-(morpholin-4-yl)ethoxy]phenyl}propyl (2S)-1-[(2S,3R)-2-cyclohexyl-3-hydroxybutanoyl]piperidine-2-carboxylate

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsISOMERASE / Fk-506 binding domain / Hsp90 cochaperone / immunophiline / peptidyl-prolyl isomerase / ligand selectivity

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