Chlorine in PDB 6o0l: Crystal Structure of Bcl-2 G101V Mutation with Venetoclax

The structure of Crystal Structure of Bcl-2 G101V Mutation with Venetoclax, PDB code: 6o0l 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)	47.51 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	33.147, 82.005, 47.508, 90.00, 90.08, 90.00
R / Rfree (%)	19.5 / 22.7

The binding sites of Chlorine atom in the Crystal Structure of Bcl-2 G101V Mutation with Venetoclax (pdb code 6o0l). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Bcl-2 G101V Mutation with Venetoclax, PDB code: 6o0l:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Bcl-2 G101V 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 G101V Mutation with Venetoclax within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:51.1 occ:1.00 CL A:LBM301 0.0 51.1 1.0 C10 A:LBM301 1.7 35.2 1.0 C9 A:LBM301 2.7 30.4 1.0 C11 A:LBM301 2.7 36.1 1.0 CG A:GLU152 3.3 52.8 1.0 CG2 A:VAL156 3.4 49.1 1.0 N A:PHE153 3.7 29.8 1.0 CA A:PHE153 3.7 34.9 1.0 C A:GLU152 3.8 39.6 1.0 O A:GLU152 3.9 32.4 1.0 CD1 A:PHE112 4.0 0.6 1.0 C12 A:LBM301 4.0 38.5 1.0 C8 A:LBM301 4.0 28.6 1.0 CB A:GLU152 4.0 34.8 1.0 CB A:PHE153 4.3 34.2 1.0 CA A:PHE112 4.3 93.4 1.0 CB A:PHE112 4.5 0.1 1.0 CE1 A:PHE104 4.5 45.6 1.0 C7 A:LBM301 4.5 36.6 1.0 CD A:GLU152 4.5 64.3 1.0 CA A:GLU152 4.6 36.2 1.0 CG A:PHE112 4.7 0.4 1.0 O A:ALA149 4.7 31.0 1.0 CB A:VAL156 4.7 43.8 1.0 N A:PHE112 4.8 90.8 1.0 CG A:MET115 4.8 78.3 1.0 OE2 A:GLU152 4.8 71.8 1.0 CB A:MET115 4.9 71.8 1.0 CE1 A:PHE112 4.9 0.3 1.0 CD1 A:PHE153 5.0 37.0 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Bcl-2 G101V 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 G101V Mutation with Venetoclax within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:71.5 occ:1.00 NH1 A:ARG183 2.5 86.8 1.0 O1 A:PEG303 2.7 50.9 1.0 ND2 A:ASN182 2.8 28.7 1.0 CA A:GLU179 3.6 31.8 1.0 CZ A:ARG183 3.7 83.2 1.0 CB A:ASN182 3.7 35.4 1.0 CG A:ASN182 3.7 34.9 1.0 C1 A:PEG303 3.9 56.8 1.0 N A:GLU179 4.1 24.9 1.0 NH2 A:ARG183 4.1 81.8 1.0 CB A:GLU179 4.1 27.8 1.0 O A:THR178 4.2 30.4 1.0 C A:THR178 4.3 33.4 1.0 CG A:GLU179 4.4 53.0 1.0 CG2 A:THR178 4.6 31.9 1.0 C A:GLU179 4.7 20.8 1.0 O A:GLU179 4.7 33.0 1.0 NE A:ARG183 4.7 74.4 1.0 OD1 A:ASN182 4.9 32.1 1.0 C2 A:PEG303 5.0 54.6 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Bcl-2 G101V Mutation with Venetoclax


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Bcl-2 G101V Mutation with Venetoclax within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl301 b:55.7 occ:1.00 CL C:LBM301 0.0 55.7 1.0 C10 C:LBM301 1.7 43.5 1.0 C11 C:LBM301 2.7 34.9 1.0 C9 C:LBM301 2.7 32.7 1.0 CG C:GLU152 3.4 58.5 1.0 N C:PHE153 3.5 26.9 1.0 CG2 C:VAL156 3.5 48.8 1.0 CA C:PHE153 3.6 33.7 1.0 C C:GLU152 3.6 37.4 1.0 O C:GLU152 3.7 37.8 1.0 CD1 C:PHE112 3.9 0.8 1.0 C12 C:LBM301 4.0 38.1 1.0 C8 C:LBM301 4.0 25.6 1.0 CB C:GLU152 4.0 43.1 1.0 CB C:PHE153 4.1 37.3 1.0 CA C:PHE112 4.4 88.5 1.0 CA C:GLU152 4.5 38.5 1.0 CE2 C:PHE104 4.5 41.2 1.0 C7 C:LBM301 4.5 37.7 1.0 CE1 C:PHE112 4.6 0.4 1.0 O C:ALA149 4.6 26.3 1.0 CD C:GLU152 4.6 68.8 1.0 CB C:PHE112 4.7 95.3 1.0 CG C:PHE112 4.7 0.9 1.0 CB C:VAL156 4.8 39.2 1.0 C C:PHE153 4.9 27.8 1.0 CD1 C:PHE153 4.9 36.5 1.0 N C:PHE112 4.9 91.9 1.0 CG C:MET115 5.0 78.2 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Bcl-2 G101V Mutation with Venetoclax


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Bcl-2 G101V Mutation with Venetoclax within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl304 b:66.3 occ:1.00 NH1 C:ARG183 2.4 88.9 1.0 O4 C:PEG303 2.8 69.7 1.0 ND2 C:ASN182 2.9 33.9 1.0 CZ C:ARG183 3.4 87.3 1.0 CB C:ASN182 3.6 29.1 1.0 CA C:GLU179 3.6 30.9 1.0 CG C:ASN182 3.8 33.4 1.0 NH2 C:ARG183 3.9 83.5 1.0 CB C:GLU179 4.1 26.6 1.0 C4 C:PEG303 4.2 70.9 1.0 N C:GLU179 4.2 27.1 1.0 O C:THR178 4.2 26.3 1.0 CG C:GLU179 4.3 56.1 1.0 C C:THR178 4.5 33.3 1.0 NE C:ARG183 4.5 86.6 1.0 O C:GLU179 4.5 26.7 1.0 C C:GLU179 4.6 25.9 1.0 CD C:ARG183 4.8 78.5 1.0 CG C:ARG183 4.8 65.6 1.0 CG2 C:THR178 4.9 29.0 1.0 C3 C:PEG303 4.9 72.3 1.0 OD1 C:ASN182 5.0 36.1 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