The FK1 domain of FKBP51 in complex with (2R,5S,12R)-12-cyclohexyl-2- [2-(3,4-DIMETHOXYPHENYL)ETHYL]-15,15,16-trimethyl-3,19-dioxa-10,13, 16-TRIAZATRICYCLO[18.3.1.0^5,^10]TETRACOSA-1(24),20,22-triene-4,11, 14,17-tetrone

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 33% strand (DSSP).

Ligands and binding sites

• S8N · (2~{R},5~{S},12~{R})-12-cyclohexyl-2-[2-(3,4-dimethoxyphenyl)ethyl]-15,15,16-trimethyl-3,19-dioxa-10,13,16-triazatricyclo[18.3.1.0^{5,10}]tetracosa-1(24),20,22-triene-4,11,14,17-tetrone · 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, 0 with a druggability of 0.5 or more.

Compared structures

• 7AWF · The Fk1 domain of FKBP51 in complex with (2R,5S,12R)-12-cyclohexyl-2-[2-(3,4-dimethoxyphen… · 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 0.95

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 7AWF · PDBe 7AWF · UniProt Q13451