The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-[(3,5- DICHLOROPHENYL)SULFONYL]-5-[(1R)-1,2-dihydroxyethyl]-3-[2-(3,4- DIMETHOXYPHENOXY)ETHYL]-3,10-DIAZABICYCLO[4.3.1]DECAN-2-one

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 38% strand (DSSP).

Ligands and binding sites

• 3JQ · (1S,5S,6R)-10-[(3,5-dichlorophenyl)sulfonyl]-5-[(1R)-1,2-dihydroxyethyl]-3-[2-(3,4-dimethoxyphenoxy)ethyl]-3,10-diazabicyclo[4.3.1]decan-2-one · ligand · 2 copies · chains A, E
• ACT · Acetate ion · additive · 2 copies · chains E

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.

Interfaces

1 interface between chains.

• A–E · 212 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

• 4W9O · The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-[(3,5-dichlorophenyl)sulfonyl]-5-[(… · 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 E against A, TM-score 0.98

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 4W9O · PDBe 4W9O · UniProt Q13451