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TitleStructure-Based Design of Ultrapotent Tricyclic Ligands for FK506-Binding Proteins.
Journal, issue, pagesChemistry, Vol. 30, Page e202401405-e202401405, Year 2024
Publish dateApr 9, 2024 (structure data deposition date)
AuthorsKrajczy, P. / Meyners, C. / Repity, M.L. / Hausch, F.
External linksChemistry / PubMed:38837733
MethodsX-ray diffraction
Resolution1.16 Å
Structure data

PDB-9ey3:
The FK1 domain of FKBP51 in complex with (3S,11S,11aS)-12-((3,5-dichlorophenyl)sulfonyl)-5-oxo-11-vinyldecahydro-1H-6,10-epiminopyrrolo[1,2-a]azonine-3-carboxylic acid
Method: X-RAY DIFFRACTION / Resolution: 1.16 Å

PDB-9ey4:
The FK1 domain of FKBP51 in complex with (3S,11S)-12-((3,5-dichlorophenyl)sulfonyl)-5-oxo-11-vinyldecahydro-1H-6,10-epiminopyrrolo[1,2-a]azonine-3-carboxamide
Method: X-RAY DIFFRACTION / Resolution: 1.16 Å

Chemicals

PDB-1h70:
DDAH FROM PSEUDOMONAS AERUGINOSA. C249S MUTANT COMPLEXED WITH CITRULLINE

ChemComp-HOH:
WATER

PDB-1h78:
STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES: NRDD IN COMPLEX WITH DCTP.

Source
  • homo sapiens (human)
KeywordsISOMERASE / FKBP51 / Inhibitor / Complex

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