FKBP12 in complex with the bmp potentiator compound 8 at 1.12A resolution

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 40% strand (DSSP).

Ligands and binding sites

• OP8 · (1aR,3R,5S,6R,7S,9R,10R,17aS,20S,21R,22S,25R,25aR)-25-Ethyl-10,22-dihydroxy-20-{(1E)-1-[(1R,3R,4R)-4-hydroxy-3-methoxycyclohexyl]prop-1-en-2-yl}-5,7-dimethoxy-1a,3,9,21-tetramethyloctadecahydro-2H-6,10-epoxyoxireno[p]pyrido[2,1-c][1,4]oxazacyclotricosine-11,12,18,24(1aH,14H)-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

• 6YF1 · FKBP12 in complex with the BMP potentiator compound 8 at 1.12A resolution · the same entry in another collection · chain A against A, TM-score 1.00
• P62942 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP1A (P62942) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P62942
• Elsewhere: RCSB PDB 6YF1 · PDBe 6YF1 · UniProt P62942