Chlorine in PDB 6o0m: Crystal Structure of Bcl-2 F104L Mutation with Venetoclax
Protein crystallography data
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
|
Chlorine Binding Sites:
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 6o0m
Go back to
Chlorine Binding Sites List in 6o0m
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 6o0m
Go back to
Chlorine Binding Sites List in 6o0m
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
|
|
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 Dec 12 13:25:33 2020
|