› 9ey4

X-ray diffraction
1.16Å resolution

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

Released:
DOI: 10.2210/pdb9ey4/pdb
PDB entry 9ey4 coloured by chain, front view.
PDB entry 9ey4 coloured by chain, side view.
PDB entry 9ey4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-Based Design of Ultrapotent Tricyclic Ligands for FK506-Binding proteins.
Krajczy P, Meyners C, Repity M, Hausch F
Chemistry e202401405 (2024)
PMID: 38837733

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171693 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP5 Chain: A
Molecule details ›
Chain: A
Length: 128 amino acids
Theoretical weight: 14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: Q13451 (Residues: 16-140; Coverage: 27%)
Gene names: AIG6, FKBP5, FKBP51
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase

Ligands and Environments

1 bound ligand:
Ligand A1H78 1 x A1H78
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 42.137Å b: 54.524Å c: 56.232Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.144 0.142 0.169
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

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