› 5dit

X-ray diffraction
2.25Å resolution

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

Released:
DOI: 10.2210/pdb5dit/pdb
PDB entry 5dit coloured by chain, front view.
PDB entry 5dit coloured by chain, side view.
PDB entry 5dit coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-Affinity Relationship Analysis of Selective FKBP51 Ligands.
Feng X, Sippel C, Bracher A, Hausch F
J Med Chem 58 7796-806 (2015)
PMID: 26419422

Function and Biology Details

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

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: 14.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13451 (Residues: 16-140; Coverage: 27%)
Gene names: AIG6, FKBP5, FKBP51
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

1 bound ligand:
Ligand 5B8 1 x 5B8
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 43.371Å b: 50.22Å c: 61.811Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.211 0.284
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds.
Dunyak et al. (2016)
5 more

1 mention without citation

Discovery of pentapeptide-inhibitor hits targeting FKBP51 by combining computational modeling and X-ray crystallography.
Han et al. (2021)