Fluorine in PDB 8szm: Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
Enzymatic activity of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
All present enzymatic activity of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12:
3.4.21.92;
Protein crystallography data
The structure of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12, PDB code: 8szm
was solved by
M.F.Mabanglo,
W.A.Houry,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
79.83 /
2.35
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
93.968,
187.589,
169.408,
90,
93.72,
90
|
R / Rfree (%)
|
20.4 /
26
|
Fluorine Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
27;
Binding sites:
The binding sites of Fluorine atom in the Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
(pdb code 8szm). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 27 binding sites of Fluorine where determined in the
Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12, PDB code: 8szm:
Jump to Fluorine binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Fluorine binding site 1 out
of 27 in 8szm
Go back to
Fluorine Binding Sites List in 8szm
Fluorine binding site 1 out
of 27 in the Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:F301
b:77.7
occ:1.00
|
F08
|
G:X3O301
|
0.0
|
77.7
|
1.0
|
C07
|
G:X3O301
|
1.4
|
76.1
|
1.0
|
F10
|
G:X3O301
|
2.2
|
77.0
|
1.0
|
F09
|
G:X3O301
|
2.2
|
76.9
|
1.0
|
C06
|
G:X3O301
|
2.4
|
76.8
|
1.0
|
CE2
|
G:TYR76
|
3.0
|
54.9
|
1.0
|
C11
|
G:X3O301
|
3.3
|
77.5
|
1.0
|
C05
|
G:X3O301
|
3.3
|
80.1
|
1.0
|
OH
|
G:TYR76
|
3.7
|
61.5
|
1.0
|
CZ
|
G:TYR76
|
3.8
|
55.1
|
1.0
|
CD1
|
G:LEU128
|
3.8
|
48.5
|
0.9
|
CD2
|
G:TYR76
|
3.9
|
48.7
|
1.0
|
OG1
|
A:THR93
|
4.1
|
44.6
|
1.0
|
N12
|
G:X3O301
|
4.5
|
80.0
|
1.0
|
C04
|
G:X3O301
|
4.5
|
80.5
|
1.0
|
CD2
|
A:LEU62
|
4.6
|
51.6
|
1.0
|
CG
|
G:LEU128
|
4.7
|
45.5
|
1.0
|
CG2
|
G:ILE104
|
4.7
|
47.0
|
1.0
|
CD2
|
G:LEU128
|
4.7
|
48.5
|
1.0
|
CD1
|
A:LEU62
|
4.7
|
49.2
|
1.0
|
SD
|
G:MET106
|
4.9
|
49.4
|
1.0
|
CB
|
A:THR93
|
4.9
|
41.0
|
1.0
|
CD2
|
A:PHE96
|
4.9
|
59.6
|
1.0
|
CG1
|
A:VAL58
|
5.0
|
42.5
|
1.0
|
CA
|
A:THR93
|
5.0
|
46.1
|
1.0
|
C03
|
G:X3O301
|
5.0
|
82.1
|
1.0
|
|
Fluorine binding site 2 out
of 27 in 8szm
Go back to
Fluorine Binding Sites List in 8szm
Fluorine binding site 2 out
of 27 in the Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:F301
b:76.9
occ:1.00
|
F09
|
G:X3O301
|
0.0
|
76.9
|
1.0
|
C07
|
G:X3O301
|
1.4
|
76.1
|
1.0
|
F10
|
G:X3O301
|
2.2
|
77.0
|
1.0
|
F08
|
G:X3O301
|
2.2
|
77.7
|
1.0
|
C06
|
G:X3O301
|
2.4
|
76.8
|
1.0
|
C11
|
G:X3O301
|
2.9
|
77.5
|
1.0
|
CD2
|
A:PHE96
|
2.9
|
59.6
|
1.0
|
CG
|
A:PHE96
|
3.1
|
55.4
|
1.0
|
CB
|
A:PHE96
|
3.3
|
53.3
|
1.0
|
C05
|
G:X3O301
|
3.6
|
80.1
|
1.0
|
CE2
|
A:PHE96
|
3.7
|
64.8
|
1.0
|
CD1
|
A:PHE96
|
4.0
|
57.7
|
1.0
|
CD1
|
G:LEU128
|
4.1
|
48.5
|
0.9
|
CA
|
A:THR93
|
4.1
|
46.1
|
1.0
|
N12
|
G:X3O301
|
4.2
|
80.0
|
1.0
|
OG1
|
A:THR93
|
4.4
|
44.6
|
1.0
|
CZ
|
A:PHE96
|
4.5
|
62.6
|
1.0
|
CD2
|
A:LEU62
|
4.5
|
51.6
|
1.0
|
CG2
|
A:THR93
|
4.6
|
37.0
|
1.0
|
O
|
A:THR93
|
4.6
|
47.6
|
1.0
|
CG2
|
A:ILE97
|
4.6
|
50.9
|
1.0
|
CE1
|
A:PHE96
|
4.6
|
55.3
|
1.0
|
CB
|
A:THR93
|
4.6
|
41.0
|
1.0
|
CA
|
A:PHE96
|
4.7
|
55.4
|
1.0
|
O
|
A:ASP92
|
4.7
|
50.8
|
1.0
|
C04
|
G:X3O301
|
4.8
|
80.5
|
1.0
|
C
|
A:THR93
|
4.9
|
46.3
|
1.0
|
N
|
A:ILE97
|
4.9
|
49.8
|
1.0
|
N
|
A:THR93
|
4.9
|
41.7
|
1.0
|
C03
|
G:X3O301
|
5.0
|
82.1
|
1.0
|
CD2
|
G:LEU128
|
5.0
|
48.5
|
1.0
|
OH
|
G:TYR76
|
5.0
|
61.5
|
1.0
|
|
Fluorine binding site 3 out
of 27 in 8szm
Go back to
Fluorine Binding Sites List in 8szm
Fluorine binding site 3 out
of 27 in the Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:F301
b:77.0
occ:1.00
|
F10
|
G:X3O301
|
0.0
|
77.0
|
1.0
|
C07
|
G:X3O301
|
1.4
|
76.1
|
1.0
|
F09
|
G:X3O301
|
2.2
|
76.9
|
1.0
|
F08
|
G:X3O301
|
2.2
|
77.7
|
1.0
|
C06
|
G:X3O301
|
2.4
|
76.8
|
1.0
|
C05
|
G:X3O301
|
2.8
|
80.1
|
1.0
|
CD2
|
G:LEU128
|
3.1
|
48.5
|
1.0
|
CD1
|
G:LEU128
|
3.2
|
48.5
|
0.9
|
C11
|
G:X3O301
|
3.6
|
77.5
|
1.0
|
CG
|
G:LEU128
|
3.6
|
45.5
|
1.0
|
CD1
|
G:LEU203
|
3.7
|
57.4
|
1.0
|
CG
|
A:PHE96
|
3.8
|
55.4
|
1.0
|
CD1
|
A:PHE96
|
4.0
|
57.7
|
1.0
|
CD2
|
A:PHE96
|
4.0
|
59.6
|
1.0
|
CG2
|
G:ILE104
|
4.1
|
47.0
|
1.0
|
C04
|
G:X3O301
|
4.1
|
80.5
|
1.0
|
CB
|
A:PHE96
|
4.3
|
53.3
|
1.0
|
CE1
|
A:PHE96
|
4.3
|
55.3
|
1.0
|
CE2
|
A:PHE96
|
4.3
|
64.8
|
1.0
|
CE2
|
G:TYR76
|
4.5
|
54.9
|
1.0
|
CZ
|
A:PHE96
|
4.5
|
62.6
|
1.0
|
CB
|
G:LEU203
|
4.6
|
43.3
|
1.0
|
N12
|
G:X3O301
|
4.7
|
80.0
|
1.0
|
CG
|
G:LEU203
|
4.8
|
53.3
|
1.0
|
OH
|
G:TYR76
|
4.9
|
61.5
|
1.0
|
C03
|
G:X3O301
|
4.9
|
82.1
|
1.0
|
|
Fluorine binding site 4 out
of 27 in 8szm
Go back to
Fluorine Binding Sites List in 8szm
Fluorine binding site 4 out
of 27 in the Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 4 of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:F301
b:86.9
occ:1.00
|
F22
|
G:X3O301
|
0.0
|
86.9
|
1.0
|
C21
|
G:X3O301
|
1.4
|
90.7
|
1.0
|
F24
|
G:X3O301
|
2.2
|
87.0
|
1.0
|
F23
|
G:X3O301
|
2.2
|
80.9
|
1.0
|
C20
|
G:X3O301
|
2.4
|
90.7
|
1.0
|
C25
|
G:X3O301
|
2.8
|
82.3
|
1.0
|
NH2
|
G:ARG36
|
3.0
|
81.6
|
1.0
|
NE
|
G:ARG36
|
3.4
|
77.3
|
1.0
|
CZ
|
G:ARG36
|
3.4
|
80.7
|
1.0
|
CD1
|
A:PHE63
|
3.5
|
63.1
|
1.0
|
CB
|
A:ALA66
|
3.6
|
59.4
|
1.0
|
CE1
|
A:PHE63
|
3.7
|
63.3
|
1.0
|
C19
|
G:X3O301
|
3.7
|
88.0
|
1.0
|
C26
|
G:X3O301
|
4.1
|
84.0
|
1.0
|
NH1
|
G:ARG36
|
4.3
|
79.0
|
1.0
|
O
|
A:PHE63
|
4.3
|
57.3
|
1.0
|
CG
|
G:ARG36
|
4.4
|
66.8
|
1.0
|
CD
|
G:ARG36
|
4.4
|
69.5
|
1.0
|
OE2
|
G:GLU40
|
4.4
|
74.4
|
1.0
|
CG
|
A:PHE63
|
4.6
|
56.0
|
1.0
|
N
|
A:GLU67
|
4.6
|
65.2
|
1.0
|
S18
|
G:X3O301
|
4.6
|
102.4
|
1.0
|
CG
|
A:GLU67
|
4.7
|
65.3
|
1.0
|
CA
|
A:PHE63
|
4.7
|
56.7
|
1.0
|
C
|
A:ALA66
|
4.7
|
59.1
|
1.0
|
C28
|
G:X3O301
|
4.8
|
80.0
|
1.0
|
CA
|
A:ALA66
|
4.8
|
57.8
|
1.0
|
CZ
|
A:PHE63
|
4.9
|
55.8
|
1.0
|
CD
|
G:GLU40
|
4.9
|
80.2
|
1.0
|
C27
|
G:X3O301
|
5.0
|
85.3
|
1.0
|
|
Fluorine binding site 5 out
of 27 in 8szm
Go back to
Fluorine Binding Sites List in 8szm
Fluorine binding site 5 out
of 27 in the Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 5 of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:F301
b:80.9
occ:1.00
|
F23
|
G:X3O301
|
0.0
|
80.9
|
1.0
|
C21
|
G:X3O301
|
1.4
|
90.7
|
1.0
|
F24
|
G:X3O301
|
2.2
|
87.0
|
1.0
|
F22
|
G:X3O301
|
2.2
|
86.9
|
1.0
|
C20
|
G:X3O301
|
2.4
|
90.7
|
1.0
|
S18
|
G:X3O301
|
2.9
|
102.4
|
1.0
|
C19
|
G:X3O301
|
2.9
|
88.0
|
1.0
|
CB
|
A:ALA66
|
3.0
|
59.4
|
1.0
|
CA
|
A:PHE63
|
3.6
|
56.7
|
1.0
|
C25
|
G:X3O301
|
3.6
|
82.3
|
1.0
|
C17
|
G:X3O301
|
3.8
|
83.5
|
1.0
|
CD1
|
A:PHE63
|
3.8
|
63.1
|
1.0
|
O
|
A:LEU62
|
4.0
|
48.8
|
1.0
|
O
|
A:PHE63
|
4.2
|
57.3
|
1.0
|
CB
|
A:PHE63
|
4.3
|
53.8
|
1.0
|
C28
|
G:X3O301
|
4.3
|
80.0
|
1.0
|
N
|
A:PHE63
|
4.4
|
55.2
|
1.0
|
CD2
|
G:LEU37
|
4.4
|
47.8
|
1.0
|
C
|
A:PHE63
|
4.4
|
55.9
|
1.0
|
CG
|
G:GLU40
|
4.4
|
74.4
|
1.0
|
CA
|
A:ALA66
|
4.5
|
57.8
|
1.0
|
C
|
A:LEU62
|
4.5
|
51.2
|
1.0
|
CG
|
A:PHE63
|
4.5
|
56.0
|
1.0
|
CD1
|
G:LEU37
|
4.6
|
56.6
|
0.7
|
CE1
|
A:PHE63
|
4.7
|
63.3
|
1.0
|
C16
|
G:X3O301
|
4.8
|
71.3
|
1.0
|
C26
|
G:X3O301
|
4.8
|
84.0
|
1.0
|
NE
|
G:ARG36
|
4.8
|
77.3
|
1.0
|
CZ
|
G:ARG36
|
4.9
|
80.7
|
1.0
|
CD
|
G:GLU40
|
4.9
|
80.2
|
1.0
|
OE2
|
G:GLU40
|
4.9
|
74.4
|
1.0
|
NH2
|
G:ARG36
|
4.9
|
81.6
|
1.0
|
CG
|
G:ARG36
|
4.9
|
66.8
|
1.0
|
|
Fluorine binding site 6 out
of 27 in 8szm
Go back to
Fluorine Binding Sites List in 8szm
Fluorine binding site 6 out
of 27 in the Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 6 of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:F301
b:87.0
occ:1.00
|
F24
|
G:X3O301
|
0.0
|
87.0
|
1.0
|
C21
|
G:X3O301
|
1.4
|
90.7
|
1.0
|
F22
|
G:X3O301
|
2.2
|
86.9
|
1.0
|
F23
|
G:X3O301
|
2.2
|
80.9
|
1.0
|
C20
|
G:X3O301
|
2.4
|
90.7
|
1.0
|
CZ
|
G:ARG36
|
3.0
|
80.7
|
1.0
|
OE2
|
G:GLU40
|
3.0
|
74.4
|
1.0
|
NE
|
G:ARG36
|
3.1
|
77.3
|
1.0
|
CG
|
G:GLU40
|
3.2
|
74.4
|
1.0
|
NH1
|
G:ARG36
|
3.3
|
79.0
|
1.0
|
C25
|
G:X3O301
|
3.3
|
82.3
|
1.0
|
C19
|
G:X3O301
|
3.3
|
88.0
|
1.0
|
O
|
G:ARG36
|
3.3
|
56.0
|
1.0
|
CD
|
G:GLU40
|
3.4
|
80.2
|
1.0
|
NH2
|
G:ARG36
|
3.4
|
81.6
|
1.0
|
CG
|
G:ARG36
|
3.7
|
66.8
|
1.0
|
CD
|
G:ARG36
|
3.7
|
69.5
|
1.0
|
S18
|
G:X3O301
|
3.8
|
102.4
|
1.0
|
C
|
G:ARG36
|
4.1
|
55.5
|
1.0
|
CD1
|
A:PHE63
|
4.3
|
63.1
|
1.0
|
OE1
|
G:GLU40
|
4.5
|
77.0
|
1.0
|
C26
|
G:X3O301
|
4.5
|
84.0
|
1.0
|
C28
|
G:X3O301
|
4.6
|
80.0
|
1.0
|
CB
|
G:GLU40
|
4.6
|
62.9
|
1.0
|
CA
|
G:LEU37
|
4.6
|
51.6
|
1.0
|
N
|
G:LEU37
|
4.6
|
53.2
|
1.0
|
CB
|
G:ARG36
|
4.7
|
61.0
|
1.0
|
CB
|
A:ALA66
|
4.8
|
59.4
|
1.0
|
CE1
|
A:PHE63
|
4.8
|
63.3
|
1.0
|
CD2
|
G:LEU37
|
4.9
|
47.8
|
1.0
|
CA
|
G:ARG36
|
4.9
|
60.4
|
1.0
|
|
Fluorine binding site 7 out
of 27 in 8szm
Go back to
Fluorine Binding Sites List in 8szm
Fluorine binding site 7 out
of 27 in the Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 7 of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:F301
b:100.1
occ:1.00
|
F37
|
G:X3O301
|
0.0
|
100.1
|
1.0
|
C36
|
G:X3O301
|
1.4
|
95.0
|
1.0
|
F39
|
G:X3O301
|
2.2
|
91.4
|
1.0
|
F38
|
G:X3O301
|
2.3
|
95.4
|
1.0
|
C35
|
G:X3O301
|
2.3
|
90.1
|
1.0
|
C40
|
G:X3O301
|
2.7
|
89.0
|
1.0
|
C34
|
G:X3O301
|
3.6
|
84.8
|
1.0
|
C41
|
G:X3O301
|
4.1
|
83.8
|
1.0
|
N33
|
G:X3O301
|
4.7
|
82.1
|
1.0
|
CZ
|
G:PHE126
|
4.8
|
48.6
|
1.0
|
C32
|
G:X3O301
|
4.9
|
84.2
|
1.0
|
|
Fluorine binding site 8 out
of 27 in 8szm
Go back to
Fluorine Binding Sites List in 8szm
Fluorine binding site 8 out
of 27 in the Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 8 of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:F301
b:95.4
occ:1.00
|
F38
|
G:X3O301
|
0.0
|
95.4
|
1.0
|
C36
|
G:X3O301
|
1.4
|
95.0
|
1.0
|
F39
|
G:X3O301
|
2.3
|
91.4
|
1.0
|
F37
|
G:X3O301
|
2.3
|
100.1
|
1.0
|
C35
|
G:X3O301
|
2.4
|
90.1
|
1.0
|
C34
|
G:X3O301
|
2.8
|
84.8
|
1.0
|
C40
|
G:X3O301
|
3.6
|
89.0
|
1.0
|
CZ
|
G:PHE126
|
4.1
|
48.6
|
1.0
|
N33
|
G:X3O301
|
4.1
|
82.1
|
1.0
|
CE2
|
G:TYR74
|
4.3
|
62.6
|
1.0
|
CE2
|
G:PHE126
|
4.4
|
50.4
|
1.0
|
C41
|
G:X3O301
|
4.7
|
83.8
|
1.0
|
OH
|
G:TYR74
|
4.7
|
75.7
|
1.0
|
C32
|
G:X3O301
|
4.9
|
84.2
|
1.0
|
|
Fluorine binding site 9 out
of 27 in 8szm
Go back to
Fluorine Binding Sites List in 8szm
Fluorine binding site 9 out
of 27 in the Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 9 of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:F301
b:91.4
occ:1.00
|
F39
|
G:X3O301
|
0.0
|
91.4
|
1.0
|
C36
|
G:X3O301
|
1.4
|
95.0
|
1.0
|
F37
|
G:X3O301
|
2.2
|
100.1
|
1.0
|
F38
|
G:X3O301
|
2.3
|
95.4
|
1.0
|
C35
|
G:X3O301
|
2.3
|
90.1
|
1.0
|
CZ
|
G:PHE126
|
2.8
|
48.6
|
1.0
|
C34
|
G:X3O301
|
3.1
|
84.8
|
1.0
|
C40
|
G:X3O301
|
3.2
|
89.0
|
1.0
|
CE1
|
G:PHE126
|
3.3
|
47.0
|
1.0
|
CE2
|
G:PHE126
|
3.4
|
50.4
|
1.0
|
CD2
|
G:LEU203
|
4.0
|
53.2
|
1.0
|
CD1
|
G:PHE126
|
4.3
|
45.2
|
1.0
|
N33
|
G:X3O301
|
4.3
|
82.1
|
1.0
|
C41
|
G:X3O301
|
4.4
|
83.8
|
1.0
|
CD2
|
G:PHE126
|
4.4
|
45.7
|
1.0
|
CG
|
G:PHE126
|
4.7
|
49.2
|
1.0
|
C32
|
G:X3O301
|
4.8
|
84.2
|
1.0
|
|
Fluorine binding site 10 out
of 27 in 8szm
Go back to
Fluorine Binding Sites List in 8szm
Fluorine binding site 10 out
of 27 in the Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 10 of Crystal Structure of E. Coli Clpp Protease in Complex with Phosphine Oxide Compound ACP6-12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
X:F301
b:64.8
occ:1.00
|
F08
|
X:X3O301
|
0.0
|
64.8
|
1.0
|
C07
|
X:X3O301
|
1.4
|
66.1
|
1.0
|
F10
|
X:X3O301
|
2.2
|
63.0
|
1.0
|
F09
|
X:X3O301
|
2.3
|
65.2
|
1.0
|
C06
|
X:X3O301
|
2.4
|
64.0
|
1.0
|
C11
|
X:X3O301
|
2.8
|
68.8
|
1.0
|
CD2
|
Y:LEU62
|
3.5
|
43.3
|
1.0
|
CD2
|
Y:PHE96
|
3.6
|
50.5
|
1.0
|
CG2
|
Y:THR93
|
3.7
|
33.4
|
1.0
|
CA
|
Y:THR93
|
3.7
|
39.4
|
1.0
|
C05
|
X:X3O301
|
3.7
|
66.7
|
1.0
|
OG1
|
Y:THR93
|
3.9
|
39.9
|
1.0
|
CB
|
Y:THR93
|
3.9
|
38.3
|
1.0
|
CB
|
Y:PHE96
|
4.0
|
43.3
|
1.0
|
CG
|
Y:PHE96
|
4.0
|
46.5
|
1.0
|
N12
|
X:X3O301
|
4.1
|
64.8
|
1.0
|
CG2
|
Y:ILE97
|
4.1
|
42.9
|
1.0
|
O
|
Y:THR93
|
4.4
|
37.0
|
1.0
|
CE2
|
Y:PHE96
|
4.5
|
55.8
|
1.0
|
CG
|
Y:LEU62
|
4.5
|
50.6
|
1.0
|
N
|
Y:THR93
|
4.6
|
39.1
|
1.0
|
C
|
Y:THR93
|
4.6
|
37.9
|
1.0
|
CD1
|
Y:LEU62
|
4.7
|
48.9
|
1.0
|
OH
|
X:TYR76
|
4.7
|
46.3
|
1.0
|
CE2
|
X:TYR76
|
4.8
|
48.0
|
1.0
|
C04
|
X:X3O301
|
4.8
|
66.5
|
1.0
|
C03
|
X:X3O301
|
4.9
|
68.5
|
1.0
|
|
Reference:
F.Lin,
M.F.Mabanglo,
J.L.Zhou,
G.Binepal,
M.M.Barghash,
K.S.Wong,
S.D.Gray-Owen,
R.A.Batey,
W.A.Houry.
Structure-Based Design and Development of Phosphine Oxides As A Novel Chemotype For Antibiotics That Dysregulate Bacterial Clpp Proteases. J.Med.Chem. 2024.
ISSN: ISSN 0022-2623
PubMed: 39221504
DOI: 10.1021/ACS.JMEDCHEM.4C00773
Page generated: Sat Sep 28 20:22:11 2024
|