The FK1 domain of FKBP51 in complex with the new synthetic ligand 2- (3-((R)-1-((S)-1-((S)-2-cyclohexyl-2-(3,4,5-TRIMETHOXYPHENYL)ACETYL) piperidine-2-carboxamido)-3-(3,4-DIMETHOXYPHENYL)PROPYL)PHENOXY) acetic acid

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 37% strand (DSSP).

Ligands and binding sites

• 5BG · {3-[(1R)-1-[({(2S)-1-[(2S)-2-cyclohexyl-2-(3,4,5-trimethoxyphenyl)acetyl]piperidin-2-yl}carbonyl)amino]-3-(3,4-dimethoxyphenyl)propyl]phenoxy}acetic acid · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Compared structures

• 5DIU · The Fk1 domain of FKBP51 in complex with the new synthetic ligand… · the same entry in another collection · chain A against A, TM-score 1.00
• Q13451 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP5 (Q13451) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q13451
• Elsewhere: RCSB PDB 5DIU · PDBe 5DIU · UniProt Q13451