Crystal structure of BCL-2 G101V mutation with venetoclax

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).

Ligands and binding sites

• LBM · 4-{4-[(4'-chloro-5,5-dimethyl[3,4,5,6-tetrahydro[1,1'-biphenyl]]-2-yl)methyl]piperazin-1-yl}-N-[(3-nitro-4-{[(oxan-4-yl)methyl]amino}phenyl)sulfonyl]-2-[(1H-pyrrolo[2,3-b]pyridin-5-yl)oxy]benzamide · ligand · 2 copies · chains A, C
• CL · Chloride ion · ion · 2 copies · chains A, C
• PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, C

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–C · 528 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

• 6O0L · crystal structure of BCL-2 G101V mutation with venetoclax · 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 A against A, TM-score 0.98
• Q07817 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 1 (Q07817) · a predicted model of the same protein · chain A against A, TM-score 0.97

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
• Every structure of UniProt Q07817
• Elsewhere: RCSB PDB 6O0L · PDBe 6O0L · UniProt P10415 · UniProt Q07817