Crystal structure of BCL-2 in complex with prodrug abbv-167

Structure

x-ray diffraction · 3 distinct chains · 77% helix, 0% strand (DSSP).

Ligands and binding sites

• XZD · Phosphoric acid mono-[5-(5-{4-[2-(4-chloro-phenyl)-4,4-dimethyl-cyclohex-1-enylmethyl]-piperazin-1-yl}-2-{3-nitro-4-[(tetrahydro-pyran-4-ylmethyl)-amino]-benzenesulfonylaminocarbonyl}-phenoxy)-pyrrolo[2,3-b]pyridin-7-ylmethyl] ester · ligand · 3 copies · chains A, B, C

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

Pockets

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

Interfaces

2 interfaces between chains.

• A–B · 215 Ų buried · 2 hydrogen bonds · protein-protein
• A–C · 204 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

• 7LHB · Crystal structure of Bcl-2 in complex with prodrug ABBV-167 · the same entry in another collection · chain A against A, TM-score 1.00
• P10415 · AlphaFold monomer V2.0 prediction for apoptosis regulator BCL-2 (P10415) · a predicted model of the same protein · chain C 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 P10415
• Elsewhere: RCSB PDB 7LHB · PDBe 7LHB · UniProt P10415