Crystal structure of BCL-2 G101V mutation with S55746

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).

Ligands and binding sites

• F3Q · ~{N}-(4-hydroxyphenyl)-3-[6-[[(3~{S})-3-(morpholin-4-ylmethyl)-3,4-dihydro-1~{H}-isoquinolin-2-yl]carbonyl]-1,3-benzodioxol-5-yl]-~{N}-phenyl-5,6,7, 8-tetrahydroindolizine-1-carboxamide · ligand · 2 copies · chains A, C

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

Pockets

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

Interfaces

1 interface between chains.

• A–C · 384 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

• 6O0O · crystal structure of BCL-2 G101V mutation with S55746 · 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 0.97
• Q07817 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 1 (Q07817) · a predicted model of the same protein · chain C 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 P10415
• Every structure of UniProt Q07817
• Elsewhere: RCSB PDB 6O0O · PDBe 6O0O · UniProt P10415 · UniProt Q07817