Chlorine in PDB 6o0p: Crystal Structure of Bcl-2 G101A Mutation with Venetoclax

The structure of Crystal Structure of Bcl-2 G101A Mutation with Venetoclax, PDB code: 6o0p 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)	43.24 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.398, 48.945, 86.474, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 23.2

The binding sites of Chlorine atom in the Crystal Structure of Bcl-2 G101A Mutation with Venetoclax (pdb code 6o0p). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Bcl-2 G101A Mutation with Venetoclax, PDB code: 6o0p:

Chlorine binding site 1 out of 1 in the Crystal Structure of Bcl-2 G101A 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 G101A Mutation with Venetoclax within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:43.2 occ:0.92 CL A:LBM301 0.0 43.2 0.9 C10 A:LBM301 1.7 32.9 0.9 C11 A:LBM301 2.7 34.5 0.9 C9 A:LBM301 2.7 27.8 0.9 C A:GLU152 3.7 23.9 1.0 N A:PHE153 3.7 24.0 1.0 CG2 A:VAL156 3.7 31.4 1.0 O A:GLU152 3.8 27.4 1.0 CB A:GLU152 3.8 24.7 1.0 CA A:PHE153 3.9 26.1 1.0 CD2 A:PHE112 4.0 62.4 1.0 C8 A:LBM301 4.0 30.2 0.9 C12 A:LBM301 4.0 33.2 0.9 CE2 A:PHE104 4.4 28.4 1.0 CA A:GLU152 4.4 24.6 1.0 CB A:PHE153 4.4 28.1 1.0 CE2 A:PHE112 4.5 66.9 1.0 C7 A:LBM301 4.5 30.4 0.9 CA A:PHE112 4.5 54.6 1.0 O A:ALA149 4.6 24.0 1.0 CG A:PHE112 4.6 64.3 1.0 CB A:VAL156 4.7 30.7 1.0 CB A:PHE112 4.8 57.5 1.0 OE1 A:GLU152 5.0 49.8 1.0

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