Chlorine in PDB 6o0m: Crystal Structure of Bcl-2 F104L Mutation with Venetoclax

The structure of Crystal Structure of Bcl-2 F104L Mutation with Venetoclax, PDB code: 6o0m was solved by R.W.Birkinshaw, C.S.Luo, P.M.Colman, P.E.Czabotar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.90 / 1.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.690, 48.270, 87.800, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 21.8

The binding sites of Chlorine atom in the Crystal Structure of Bcl-2 F104L Mutation with Venetoclax (pdb code 6o0m). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Bcl-2 F104L Mutation with Venetoclax, PDB code: 6o0m:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Bcl-2 F104L Mutation with Venetoclax


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Bcl-2 F104L Mutation with Venetoclax within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:27.3 occ:0.26 CL A:LBM301 0.0 27.3 0.3 CL A:LBM301 0.1 28.8 0.7 C10 A:LBM301 1.7 26.8 0.7 C10 A:LBM301 1.7 26.2 0.3 C11 A:LBM301 2.6 23.6 0.7 C11 A:LBM301 2.7 24.8 0.3 C9 A:LBM301 2.7 25.9 0.3 C9 A:LBM301 2.8 25.1 0.7 CE1 A:PHE112 3.4 17.0 0.6 CD1 A:PHE112 3.4 17.4 0.6 CG2 A:VAL156 3.5 19.6 1.0 CZ A:PHE112 3.6 24.9 0.6 CA A:PHE153 3.6 12.5 1.0 N A:PHE153 3.6 12.0 1.0 O A:GLU152 3.6 11.4 1.0 C A:GLU152 3.7 13.6 1.0 CG A:PHE112 3.7 17.4 0.6 CE2 A:PHE112 3.9 21.6 0.6 CD2 A:PHE112 3.9 23.3 0.6 C12 A:LBM301 3.9 26.3 0.7 C12 A:LBM301 4.0 25.3 0.3 C8 A:LBM301 4.0 25.6 0.3 C8 A:LBM301 4.0 26.6 0.7 CB A:GLU152 4.1 14.9 1.0 CB A:VAL156 4.2 18.6 1.0 CB A:PHE153 4.2 10.4 1.0 CD1 A:PHE112 4.3 21.4 0.5 C7 A:LBM301 4.5 24.1 0.7 C7 A:LBM301 4.5 25.1 0.3 CA A:GLU152 4.5 9.3 1.0 CB A:PHE112 4.5 18.6 0.6 CA A:PHE112 4.7 18.4 0.6 CD1 A:PHE153 4.8 13.3 1.0 O A:ALA149 4.8 13.1 1.0 CA A:PHE112 4.8 19.1 0.5 C A:PHE153 4.9 10.5 1.0 CG1 A:VAL156 4.9 16.9 1.0 CE1 A:PHE112 4.9 23.8 0.5 CG A:MET115 4.9 28.1 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Bcl-2 F104L Mutation with Venetoclax


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Bcl-2 F104L Mutation with Venetoclax within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:28.8 occ:0.74 CL A:LBM301 0.0 28.8 0.7 CL A:LBM301 0.1 27.3 0.3 C10 A:LBM301 1.7 26.8 0.7 C10 A:LBM301 1.8 26.2 0.3 C9 A:LBM301 2.7 25.9 0.3 C11 A:LBM301 2.7 23.6 0.7 C9 A:LBM301 2.7 25.1 0.7 C11 A:LBM301 2.8 24.8 0.3 CE1 A:PHE112 3.4 17.0 0.6 N A:PHE153 3.5 12.0 1.0 CD1 A:PHE112 3.5 17.4 0.6 CA A:PHE153 3.5 12.5 1.0 C A:GLU152 3.5 13.6 1.0 CG2 A:VAL156 3.6 19.6 1.0 O A:GLU152 3.6 11.4 1.0 CZ A:PHE112 3.6 24.9 0.6 CG A:PHE112 3.8 17.4 0.6 CE2 A:PHE112 3.9 21.6 0.6 CB A:GLU152 4.0 14.9 1.0 C8 A:LBM301 4.0 25.6 0.3 CD2 A:PHE112 4.0 23.3 0.6 C12 A:LBM301 4.0 26.3 0.7 C8 A:LBM301 4.0 26.6 0.7 C12 A:LBM301 4.0 25.3 0.3 CB A:PHE153 4.1 10.4 1.0 CB A:VAL156 4.2 18.6 1.0 CD1 A:PHE112 4.4 21.4 0.5 CA A:GLU152 4.4 9.3 1.0 C7 A:LBM301 4.5 24.1 0.7 C7 A:LBM301 4.5 25.1 0.3 O A:ALA149 4.6 13.1 1.0 CB A:PHE112 4.7 18.6 0.6 CD1 A:PHE153 4.7 13.3 1.0 C A:PHE153 4.8 10.5 1.0 CA A:PHE112 4.8 18.4 0.6 CA A:PHE112 5.0 19.1 0.5 CG A:PHE153 5.0 11.9 1.0 CG1 A:VAL156 5.0 16.9 1.0 CE1 A:PHE112 5.0 23.8 0.5

R.W.Birkinshaw, J.N.Gong, C.S.Luo, D.Lio, C.A.White, M.A.Anderson, P.Blombery, G.Lessene, I.J.Majewski, R.Thijssen, A.W.Roberts, D.C.S.Huang, P.M.Colman, P.E.Czabotar. Structures of Bcl-2 in Complex with Venetoclax Reveal the Molecular Basis of Resistance Mutations. Nat Commun V. 10 2385 2019.
ISSN: ESSN 2041-1723
PubMed: 31160589
DOI: 10.1038/S41467-019-10363-1