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Chlorine in PDB 6o0k: Crystal Structure of Bcl-2 with Venetoclax

Protein crystallography data

The structure of Crystal Structure of Bcl-2 with Venetoclax, PDB code: 6o0k 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) 43.66 / 1.62
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 33.725, 48.506, 87.316, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 20.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Bcl-2 with Venetoclax (pdb code 6o0k). 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 with Venetoclax, PDB code: 6o0k:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6o0k

Go back to Chlorine Binding Sites List in 6o0k
Chlorine binding site 1 out of 2 in the Crystal Structure of Bcl-2 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 with Venetoclax within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:24.1
occ:0.61
CL A:LBM301 0.0 24.1 0.6
CL A:LBM301 0.2 14.9 0.4
C10 A:LBM301 1.7 16.4 0.6
C10 A:LBM301 1.7 16.3 0.4
C9 A:LBM301 2.6 14.1 0.4
C9 A:LBM301 2.7 12.6 0.6
C11 A:LBM301 2.7 14.7 0.6
C11 A:LBM301 2.8 14.8 0.4
N A:PHE153 3.6 9.0 1.0
C A:GLU152 3.7 10.9 1.0
CB A:GLU152 3.7 9.7 1.0
CD1 A:PHE112 3.8 17.5 1.0
O A:GLU152 3.8 10.6 1.0
CA A:PHE153 3.8 10.5 1.0
CG2 A:VAL156 3.9 14.8 1.0
C8 A:LBM301 3.9 14.5 0.4
C8 A:LBM301 4.0 15.3 0.6
C12 A:LBM301 4.0 15.0 0.6
C12 A:LBM301 4.0 15.1 0.4
CE2 A:PHE104 4.1 12.8 1.0
CA A:GLU152 4.4 9.0 1.0
CE1 A:PHE112 4.4 20.9 1.0
CB A:PHE153 4.4 10.3 1.0
C7 A:LBM301 4.5 14.8 0.4
C7 A:LBM301 4.5 14.4 0.6
CG A:PHE112 4.5 17.9 1.0
O A:ALA149 4.5 9.9 1.0
CA A:PHE112 4.6 16.5 1.0
CB A:VAL156 4.7 10.7 1.0
CB A:PHE112 4.7 14.3 1.0
OG A:SER105 4.9 14.0 0.4
CG A:GLU152 5.0 11.2 1.0
CD2 A:PHE104 5.0 10.8 1.0

Chlorine binding site 2 out of 2 in 6o0k

Go back to Chlorine Binding Sites List in 6o0k
Chlorine binding site 2 out of 2 in the Crystal Structure of Bcl-2 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 with Venetoclax within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:14.9
occ:0.39
CL A:LBM301 0.0 14.9 0.4
CL A:LBM301 0.2 24.1 0.6
C10 A:LBM301 1.7 16.3 0.4
C10 A:LBM301 1.7 16.4 0.6
C11 A:LBM301 2.6 14.7 0.6
C11 A:LBM301 2.7 14.8 0.4
C9 A:LBM301 2.7 14.1 0.4
C9 A:LBM301 2.8 12.6 0.6
CD1 A:PHE112 3.7 17.5 1.0
CG2 A:VAL156 3.7 14.8 1.0
N A:PHE153 3.8 9.0 1.0
C A:GLU152 3.8 10.9 1.0
O A:GLU152 3.9 10.6 1.0
CA A:PHE153 3.9 10.5 1.0
CB A:GLU152 3.9 9.7 1.0
C12 A:LBM301 3.9 15.0 0.6
C12 A:LBM301 4.0 15.1 0.4
C8 A:LBM301 4.0 14.5 0.4
C8 A:LBM301 4.0 15.3 0.6
CE2 A:PHE104 4.3 12.8 1.0
CE1 A:PHE112 4.3 20.9 1.0
CG A:PHE112 4.4 17.9 1.0
CA A:PHE112 4.4 16.5 1.0
CB A:PHE153 4.5 10.3 1.0
C7 A:LBM301 4.5 14.8 0.4
C7 A:LBM301 4.5 14.4 0.6
CA A:GLU152 4.5 9.0 1.0
CB A:VAL156 4.6 10.7 1.0
CB A:PHE112 4.6 14.3 1.0
O A:ALA149 4.7 9.9 1.0
OG A:SER105 5.0 14.0 0.4

Reference:

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
Page generated: Sat Jul 12 17:36:16 2025

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