Fluorine in PDB 6g83: Crystal Structure of M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz)
Enzymatic activity of Crystal Structure of M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz)
All present enzymatic activity of Crystal Structure of M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz):
1.1.98.3;
Protein crystallography data
The structure of Crystal Structure of M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz), PDB code: 6g83
was solved by
J.Piton,
V.Makarov,
S.T.Cole,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
49.18 /
2.40
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
78.164,
84.024,
81.666,
90.00,
103.98,
90.00
|
|
R / Rfree (%)
|
19.8 /
22.6
|
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz)
(pdb code 6g83). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the
Crystal Structure of M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz), PDB code: 6g83:
Jump to Fluorine binding site number:
1;
2;
3;
4;
5;
6;
Fluorine binding site 1 out
of 6 in 6g83
Go back to
Fluorine Binding Sites List in 6g83
Fluorine binding site 1 out
of 6 in the Crystal Structure of M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz)
 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 M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F502
b:56.2
occ:1.00
|
F16
|
A:EQ8502
|
0.0
|
56.2
|
1.0
|
|
C15
|
A:EQ8502
|
1.3
|
58.6
|
1.0
|
|
F18
|
A:EQ8502
|
2.1
|
56.5
|
1.0
|
|
F17
|
A:EQ8502
|
2.1
|
58.8
|
1.0
|
|
C13
|
A:EQ8502
|
2.4
|
58.0
|
1.0
|
|
H141
|
A:EQ8502
|
2.5
|
65.1
|
1.0
|
|
HB3
|
A:LYS367
|
2.8
|
55.9
|
1.0
|
|
C14
|
A:EQ8502
|
2.8
|
59.1
|
1.0
|
|
HD22
|
A:ASN385
|
2.8
|
48.0
|
1.0
|
|
HD3
|
A:LYS367
|
3.1
|
57.1
|
1.0
|
|
HD21
|
A:ASN385
|
3.1
|
48.0
|
1.0
|
|
ND2
|
A:ASN385
|
3.2
|
43.6
|
1.0
|
|
HE1
|
A:PHE369
|
3.2
|
45.7
|
1.0
|
|
HD2
|
A:LYS367
|
3.5
|
57.1
|
1.0
|
|
HD2
|
A:HIS132
|
3.5
|
50.0
|
1.0
|
|
CB
|
A:LYS367
|
3.5
|
49.0
|
1.0
|
|
HB2
|
A:LYS367
|
3.5
|
55.9
|
1.0
|
|
CD
|
A:LYS367
|
3.6
|
48.9
|
1.0
|
|
C12
|
A:EQ8502
|
3.7
|
57.4
|
1.0
|
|
HG12
|
A:VAL365
|
3.8
|
61.2
|
1.0
|
|
H121
|
A:EQ8502
|
3.9
|
61.7
|
1.0
|
|
CE1
|
A:PHE369
|
4.0
|
40.5
|
1.0
|
|
CG
|
A:LYS367
|
4.1
|
47.3
|
1.0
|
|
CD2
|
A:HIS132
|
4.1
|
42.1
|
1.0
|
|
HZ
|
A:PHE369
|
4.2
|
36.0
|
1.0
|
|
C04
|
A:EQ8502
|
4.2
|
58.9
|
1.0
|
|
CG
|
A:ASN385
|
4.3
|
41.4
|
1.0
|
|
HG2
|
A:LYS367
|
4.3
|
52.7
|
1.0
|
|
NE2
|
A:HIS132
|
4.3
|
42.1
|
1.0
|
|
HB3
|
A:ASN385
|
4.4
|
34.4
|
1.0
|
|
HG11
|
A:VAL365
|
4.5
|
61.2
|
1.0
|
|
CZ
|
A:PHE369
|
4.5
|
35.9
|
1.0
|
|
CG1
|
A:VAL365
|
4.6
|
52.1
|
1.0
|
|
HE22
|
A:GLN336
|
4.6
|
42.7
|
1.0
|
|
HE21
|
A:GLN336
|
4.8
|
42.7
|
1.0
|
|
CA
|
A:LYS367
|
4.8
|
47.5
|
1.0
|
|
O
|
A:GLY133
|
4.8
|
41.0
|
1.0
|
|
HA
|
A:LYS134
|
4.8
|
49.9
|
1.0
|
|
C11
|
A:EQ8502
|
4.9
|
61.9
|
1.0
|
|
N
|
A:LYS367
|
4.9
|
43.2
|
1.0
|
|
HB2
|
A:SER228
|
4.9
|
44.3
|
1.0
|
|
HG3
|
A:LYS367
|
4.9
|
52.7
|
1.0
|
|
NE2
|
A:GLN336
|
4.9
|
39.3
|
1.0
|
|
CB
|
A:ASN385
|
4.9
|
37.3
|
1.0
|
|
Fluorine binding site 2 out
of 6 in 6g83
Go back to
Fluorine Binding Sites List in 6g83
Fluorine binding site 2 out
of 6 in the Crystal Structure of M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz)
 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 M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F502
b:58.8
occ:1.00
|
F17
|
A:EQ8502
|
0.0
|
58.8
|
1.0
|
|
C15
|
A:EQ8502
|
1.4
|
58.6
|
1.0
|
|
F16
|
A:EQ8502
|
2.1
|
56.2
|
1.0
|
|
F18
|
A:EQ8502
|
2.1
|
56.5
|
1.0
|
|
C13
|
A:EQ8502
|
2.4
|
58.0
|
1.0
|
|
H121
|
A:EQ8502
|
2.7
|
61.7
|
1.0
|
|
HD2
|
A:LYS367
|
2.8
|
57.1
|
1.0
|
|
C12
|
A:EQ8502
|
2.9
|
57.4
|
1.0
|
|
HG2
|
A:LYS134
|
3.1
|
75.9
|
1.0
|
|
HB2
|
A:LYS367
|
3.1
|
55.9
|
1.0
|
|
HB2
|
A:SER228
|
3.2
|
44.3
|
1.0
|
|
HB3
|
A:SER228
|
3.3
|
44.3
|
1.0
|
|
HA
|
A:LYS134
|
3.4
|
49.9
|
1.0
|
|
HG12
|
A:VAL365
|
3.4
|
61.2
|
1.0
|
|
HB3
|
A:LYS367
|
3.4
|
55.9
|
1.0
|
|
HD3
|
A:LYS367
|
3.5
|
57.1
|
1.0
|
|
CD
|
A:LYS367
|
3.5
|
48.9
|
1.0
|
|
C14
|
A:EQ8502
|
3.6
|
59.1
|
1.0
|
|
HG11
|
A:VAL365
|
3.7
|
61.2
|
1.0
|
|
CB
|
A:LYS367
|
3.7
|
49.0
|
1.0
|
|
CB
|
A:SER228
|
3.7
|
43.4
|
1.0
|
|
H141
|
A:EQ8502
|
3.8
|
65.1
|
1.0
|
|
CG1
|
A:VAL365
|
4.0
|
52.1
|
1.0
|
|
CG
|
A:LYS134
|
4.0
|
57.8
|
1.0
|
|
HZ3
|
A:LYS134
|
4.1
|
78.5
|
1.0
|
|
CA
|
A:LYS134
|
4.2
|
45.2
|
1.0
|
|
CG
|
A:LYS367
|
4.2
|
47.3
|
1.0
|
|
HG3
|
A:LYS134
|
4.2
|
75.9
|
1.0
|
|
HZ2
|
A:LYS134
|
4.3
|
78.5
|
1.0
|
|
N
|
A:LYS134
|
4.3
|
41.7
|
1.0
|
|
C11
|
A:EQ8502
|
4.3
|
61.9
|
1.0
|
|
HA
|
A:SER228
|
4.3
|
48.7
|
1.0
|
|
HG13
|
A:VAL365
|
4.4
|
61.2
|
1.0
|
|
C
|
A:GLY133
|
4.4
|
40.8
|
1.0
|
|
O
|
A:GLY133
|
4.4
|
41.0
|
1.0
|
|
O
|
A:SER227
|
4.6
|
45.1
|
1.0
|
|
NZ
|
A:LYS134
|
4.6
|
60.0
|
1.0
|
|
HD2
|
A:HIS132
|
4.6
|
50.0
|
1.0
|
|
CB
|
A:LYS134
|
4.6
|
50.0
|
1.0
|
|
CA
|
A:SER228
|
4.7
|
45.9
|
1.0
|
|
H
|
A:LYS134
|
4.7
|
43.4
|
1.0
|
|
HD22
|
A:ASN385
|
4.7
|
48.0
|
1.0
|
|
OG
|
A:SER228
|
4.7
|
50.3
|
1.0
|
|
HE1
|
A:PHE369
|
4.7
|
45.7
|
1.0
|
|
HA2
|
A:GLY133
|
4.7
|
43.5
|
1.0
|
|
HG3
|
A:LYS367
|
4.8
|
52.7
|
1.0
|
|
HE2
|
A:LYS367
|
4.8
|
53.2
|
1.0
|
|
CE
|
A:LYS367
|
4.8
|
47.2
|
1.0
|
|
C04
|
A:EQ8502
|
4.8
|
58.9
|
1.0
|
|
O
|
A:PHE366
|
4.8
|
47.4
|
1.0
|
|
HG2
|
A:LYS367
|
4.9
|
52.7
|
1.0
|
|
HB3
|
A:LYS134
|
4.9
|
59.4
|
1.0
|
|
HG
|
A:SER228
|
4.9
|
58.3
|
1.0
|
|
HZ3
|
A:LYS367
|
5.0
|
47.5
|
1.0
|
|
Fluorine binding site 3 out
of 6 in 6g83
Go back to
Fluorine Binding Sites List in 6g83
Fluorine binding site 3 out
of 6 in the Crystal Structure of M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz)
 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 M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F502
b:56.5
occ:1.00
|
F18
|
A:EQ8502
|
0.0
|
56.5
|
1.0
|
|
C15
|
A:EQ8502
|
1.3
|
58.6
|
1.0
|
|
F16
|
A:EQ8502
|
2.1
|
56.2
|
1.0
|
|
F17
|
A:EQ8502
|
2.1
|
58.8
|
1.0
|
|
C13
|
A:EQ8502
|
2.4
|
58.0
|
1.0
|
|
HD2
|
A:HIS132
|
2.6
|
50.0
|
1.0
|
|
HA2
|
A:GLY133
|
3.0
|
43.5
|
1.0
|
|
H121
|
A:EQ8502
|
3.1
|
61.7
|
1.0
|
|
C12
|
A:EQ8502
|
3.1
|
57.4
|
1.0
|
|
C
|
A:GLY133
|
3.2
|
40.8
|
1.0
|
|
O
|
A:GLY133
|
3.3
|
41.0
|
1.0
|
|
HD3
|
A:LYS367
|
3.4
|
57.1
|
1.0
|
|
C14
|
A:EQ8502
|
3.4
|
59.1
|
1.0
|
|
CD2
|
A:HIS132
|
3.5
|
42.1
|
1.0
|
|
HD2
|
A:LYS367
|
3.5
|
57.1
|
1.0
|
|
H141
|
A:EQ8502
|
3.5
|
65.1
|
1.0
|
|
CA
|
A:GLY133
|
3.5
|
40.0
|
1.0
|
|
HA
|
A:LYS134
|
3.7
|
49.9
|
1.0
|
|
N
|
A:LYS134
|
3.7
|
41.7
|
1.0
|
|
HE1
|
A:PHE369
|
3.8
|
45.7
|
1.0
|
|
CD
|
A:LYS367
|
3.9
|
48.9
|
1.0
|
|
N
|
A:GLY133
|
4.1
|
37.9
|
1.0
|
|
H
|
A:LYS134
|
4.1
|
43.4
|
1.0
|
|
NE2
|
A:HIS132
|
4.1
|
42.1
|
1.0
|
|
HG2
|
A:LYS134
|
4.1
|
75.9
|
1.0
|
|
O4
|
A:FAD501
|
4.2
|
45.6
|
1.0
|
|
CA
|
A:LYS134
|
4.2
|
45.2
|
1.0
|
|
HN3
|
A:FAD501
|
4.4
|
38.0
|
1.0
|
|
HA3
|
A:GLY133
|
4.4
|
43.5
|
1.0
|
|
HB3
|
A:LYS367
|
4.4
|
55.9
|
1.0
|
|
C11
|
A:EQ8502
|
4.5
|
61.9
|
1.0
|
|
H
|
A:GLY133
|
4.5
|
39.3
|
1.0
|
|
C
|
A:HIS132
|
4.6
|
34.7
|
1.0
|
|
O
|
A:HIS132
|
4.6
|
37.3
|
1.0
|
|
HG3
|
A:LYS134
|
4.6
|
75.9
|
1.0
|
|
CG
|
A:HIS132
|
4.6
|
38.5
|
1.0
|
|
C04
|
A:EQ8502
|
4.7
|
58.9
|
1.0
|
|
HE2
|
A:LYS367
|
4.7
|
53.2
|
1.0
|
|
CE1
|
A:PHE369
|
4.7
|
40.5
|
1.0
|
|
HB2
|
A:LYS367
|
4.7
|
55.9
|
1.0
|
|
CG
|
A:LYS134
|
4.8
|
57.8
|
1.0
|
|
HB2
|
A:HIS132
|
4.8
|
41.3
|
1.0
|
|
HZ
|
A:PHE369
|
4.9
|
36.0
|
1.0
|
|
CB
|
A:LYS367
|
4.9
|
49.0
|
1.0
|
|
HD21
|
A:ASN385
|
4.9
|
48.0
|
1.0
|
|
HD22
|
A:ASN385
|
4.9
|
48.0
|
1.0
|
|
CE
|
A:LYS367
|
4.9
|
47.2
|
1.0
|
|
HH
|
A:TYR314
|
4.9
|
76.6
|
1.0
|
|
CG
|
A:LYS367
|
5.0
|
47.3
|
1.0
|
|
Fluorine binding site 4 out
of 6 in 6g83
Go back to
Fluorine Binding Sites List in 6g83
Fluorine binding site 4 out
of 6 in the Crystal Structure of M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz)
 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 M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F502
b:67.5
occ:1.00
|
F16
|
B:EQ8502
|
0.0
|
67.5
|
1.0
|
|
C15
|
B:EQ8502
|
1.3
|
64.3
|
1.0
|
|
F18
|
B:EQ8502
|
2.1
|
70.7
|
1.0
|
|
F17
|
B:EQ8502
|
2.1
|
71.0
|
1.0
|
|
C13
|
B:EQ8502
|
2.4
|
66.8
|
1.0
|
|
H121
|
B:EQ8502
|
2.7
|
79.1
|
1.0
|
|
HD2
|
B:HIS132
|
2.8
|
49.1
|
1.0
|
|
HA2
|
B:GLY133
|
2.9
|
49.7
|
1.0
|
|
C12
|
B:EQ8502
|
2.9
|
69.6
|
1.0
|
|
C
|
B:GLY133
|
2.9
|
46.7
|
1.0
|
|
O
|
B:GLY133
|
3.0
|
43.9
|
1.0
|
|
HA
|
B:LYS134
|
3.2
|
56.9
|
1.0
|
|
N
|
B:LYS134
|
3.3
|
48.0
|
1.0
|
|
CA
|
B:GLY133
|
3.3
|
45.7
|
1.0
|
|
C14
|
B:EQ8502
|
3.5
|
68.1
|
1.0
|
|
H
|
B:LYS134
|
3.7
|
49.8
|
1.0
|
|
CD2
|
B:HIS132
|
3.7
|
45.4
|
1.0
|
|
H141
|
B:EQ8502
|
3.7
|
74.5
|
1.0
|
|
HG2
|
B:LYS367
|
3.8
|
58.0
|
1.0
|
|
CA
|
B:LYS134
|
3.8
|
51.6
|
1.0
|
|
HE1
|
B:PHE369
|
3.8
|
51.5
|
1.0
|
|
N
|
B:GLY133
|
4.0
|
43.5
|
1.0
|
|
HG2
|
B:LYS134
|
4.0
|
70.4
|
1.0
|
|
HZ2
|
B:LYS367
|
4.2
|
71.3
|
1.0
|
|
HA3
|
B:GLY133
|
4.2
|
49.7
|
1.0
|
|
C11
|
B:EQ8502
|
4.2
|
69.0
|
1.0
|
|
HB2
|
B:LYS367
|
4.3
|
66.5
|
1.0
|
|
H
|
B:GLY133
|
4.3
|
45.1
|
1.0
|
|
NE2
|
B:HIS132
|
4.4
|
47.0
|
1.0
|
|
HG3
|
B:LYS134
|
4.5
|
70.4
|
1.0
|
|
HB3
|
B:LYS367
|
4.5
|
66.5
|
1.0
|
|
C
|
B:HIS132
|
4.5
|
42.7
|
1.0
|
|
O4
|
B:FAD501
|
4.5
|
51.8
|
1.0
|
|
CG
|
B:LYS367
|
4.6
|
54.1
|
1.0
|
|
CG
|
B:LYS134
|
4.6
|
58.4
|
1.0
|
|
O
|
B:HIS132
|
4.6
|
40.6
|
1.0
|
|
CB
|
B:LYS367
|
4.7
|
58.5
|
1.0
|
|
C04
|
B:EQ8502
|
4.7
|
67.9
|
1.0
|
|
HN3
|
B:FAD501
|
4.7
|
48.5
|
1.0
|
|
CE1
|
B:PHE369
|
4.7
|
48.2
|
1.0
|
|
CB
|
B:LYS134
|
4.8
|
54.5
|
1.0
|
|
CG
|
B:HIS132
|
4.8
|
43.3
|
1.0
|
|
HD3
|
B:LYS367
|
4.8
|
75.4
|
1.0
|
|
HB3
|
B:SER228
|
4.9
|
42.0
|
1.0
|
|
C
|
B:LYS134
|
4.9
|
50.4
|
1.0
|
|
HB2
|
B:HIS132
|
4.9
|
41.8
|
1.0
|
|
HB2
|
B:HIS136
|
4.9
|
50.8
|
1.0
|
|
NZ
|
B:LYS367
|
5.0
|
59.8
|
1.0
|
|
C05
|
B:EQ8502
|
5.0
|
75.5
|
1.0
|
|
HG11
|
B:VAL365
|
5.0
|
72.8
|
1.0
|
|
Fluorine binding site 5 out
of 6 in 6g83
Go back to
Fluorine Binding Sites List in 6g83
Fluorine binding site 5 out
of 6 in the Crystal Structure of M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz)
 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 M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F502
b:71.0
occ:1.00
|
F17
|
B:EQ8502
|
0.0
|
71.0
|
1.0
|
|
C15
|
B:EQ8502
|
1.3
|
64.3
|
1.0
|
|
F16
|
B:EQ8502
|
2.1
|
67.5
|
1.0
|
|
F18
|
B:EQ8502
|
2.2
|
70.7
|
1.0
|
|
C13
|
B:EQ8502
|
2.4
|
66.8
|
1.0
|
|
H141
|
B:EQ8502
|
2.5
|
74.5
|
1.0
|
|
C14
|
B:EQ8502
|
2.8
|
68.1
|
1.0
|
|
HB3
|
B:LYS367
|
3.0
|
66.5
|
1.0
|
|
HE1
|
B:PHE369
|
3.0
|
51.5
|
1.0
|
|
HD2
|
B:HIS132
|
3.1
|
49.1
|
1.0
|
|
HD22
|
B:ASN385
|
3.1
|
60.7
|
1.0
|
|
HD21
|
B:ASN385
|
3.2
|
60.7
|
1.0
|
|
HG2
|
B:LYS367
|
3.3
|
58.0
|
1.0
|
|
ND2
|
B:ASN385
|
3.3
|
54.1
|
1.0
|
|
HB2
|
B:LYS367
|
3.3
|
66.5
|
1.0
|
|
CB
|
B:LYS367
|
3.5
|
58.5
|
1.0
|
|
CD2
|
B:HIS132
|
3.6
|
45.4
|
1.0
|
|
C12
|
B:EQ8502
|
3.7
|
69.6
|
1.0
|
|
HZ
|
B:PHE369
|
3.7
|
45.0
|
1.0
|
|
CE1
|
B:PHE369
|
3.7
|
48.2
|
1.0
|
|
NE2
|
B:HIS132
|
3.9
|
47.0
|
1.0
|
|
CG
|
B:LYS367
|
3.9
|
54.1
|
1.0
|
|
H121
|
B:EQ8502
|
3.9
|
79.1
|
1.0
|
|
CZ
|
B:PHE369
|
4.0
|
45.5
|
1.0
|
|
CG
|
B:ASN385
|
4.2
|
51.5
|
1.0
|
|
C04
|
B:EQ8502
|
4.3
|
67.9
|
1.0
|
|
HG12
|
B:VAL365
|
4.3
|
72.8
|
1.0
|
|
HG3
|
B:LYS367
|
4.4
|
58.0
|
1.0
|
|
HB3
|
B:ASN385
|
4.4
|
45.1
|
1.0
|
|
HE22
|
B:GLN336
|
4.5
|
46.4
|
1.0
|
|
O
|
B:GLY133
|
4.5
|
43.9
|
1.0
|
|
HZ2
|
B:LYS367
|
4.7
|
71.3
|
1.0
|
|
HA
|
B:LYS134
|
4.7
|
56.9
|
1.0
|
|
HG11
|
B:VAL365
|
4.7
|
72.8
|
1.0
|
|
HE21
|
B:GLN336
|
4.7
|
46.4
|
1.0
|
|
CD1
|
B:PHE369
|
4.8
|
51.0
|
1.0
|
|
HA2
|
B:GLY133
|
4.8
|
49.7
|
1.0
|
|
C
|
B:GLY133
|
4.8
|
46.7
|
1.0
|
|
CG
|
B:HIS132
|
4.9
|
43.3
|
1.0
|
|
HD3
|
B:LYS367
|
4.9
|
75.4
|
1.0
|
|
C11
|
B:EQ8502
|
4.9
|
69.0
|
1.0
|
|
NE2
|
B:GLN336
|
4.9
|
47.6
|
1.0
|
|
CA
|
B:LYS367
|
4.9
|
57.0
|
1.0
|
|
HD1
|
B:PHE369
|
4.9
|
57.5
|
1.0
|
|
OD1
|
B:ASN385
|
4.9
|
49.1
|
1.0
|
|
CB
|
B:ASN385
|
4.9
|
46.5
|
1.0
|
|
CG1
|
B:VAL365
|
5.0
|
63.7
|
1.0
|
|
Fluorine binding site 6 out
of 6 in 6g83
Go back to
Fluorine Binding Sites List in 6g83
Fluorine binding site 6 out
of 6 in the Crystal Structure of M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz)
 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 M. Tuberculosis DPRE1 in Complex with SPBTZ169 (Sulfonylpbtz) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F502
b:70.7
occ:1.00
|
F18
|
B:EQ8502
|
0.0
|
70.7
|
1.0
|
|
C15
|
B:EQ8502
|
1.3
|
64.3
|
1.0
|
|
F16
|
B:EQ8502
|
2.1
|
67.5
|
1.0
|
|
F17
|
B:EQ8502
|
2.2
|
71.0
|
1.0
|
|
C13
|
B:EQ8502
|
2.4
|
66.8
|
1.0
|
|
HB2
|
B:LYS367
|
2.5
|
66.5
|
1.0
|
|
H121
|
B:EQ8502
|
2.8
|
79.1
|
1.0
|
|
C12
|
B:EQ8502
|
3.0
|
69.6
|
1.0
|
|
HG2
|
B:LYS367
|
3.1
|
58.0
|
1.0
|
|
CB
|
B:LYS367
|
3.2
|
58.5
|
1.0
|
|
HB3
|
B:LYS367
|
3.3
|
66.5
|
1.0
|
|
HA
|
B:LYS134
|
3.3
|
56.9
|
1.0
|
|
HB3
|
B:SER228
|
3.4
|
42.0
|
1.0
|
|
HG12
|
B:VAL365
|
3.4
|
72.8
|
1.0
|
|
HB2
|
B:SER228
|
3.5
|
42.0
|
1.0
|
|
C14
|
B:EQ8502
|
3.5
|
68.1
|
1.0
|
|
HG11
|
B:VAL365
|
3.5
|
72.8
|
1.0
|
|
HD3
|
B:LYS367
|
3.6
|
75.4
|
1.0
|
|
CG
|
B:LYS367
|
3.6
|
54.1
|
1.0
|
|
HG2
|
B:LYS134
|
3.7
|
70.4
|
1.0
|
|
H141
|
B:EQ8502
|
3.7
|
74.5
|
1.0
|
|
CB
|
B:SER228
|
3.9
|
45.3
|
1.0
|
|
CG1
|
B:VAL365
|
3.9
|
63.7
|
1.0
|
|
CD
|
B:LYS367
|
4.1
|
62.4
|
1.0
|
|
CA
|
B:LYS134
|
4.2
|
51.6
|
1.0
|
|
HZ2
|
B:LYS367
|
4.2
|
71.3
|
1.0
|
|
HG13
|
B:VAL365
|
4.3
|
72.8
|
1.0
|
|
C11
|
B:EQ8502
|
4.3
|
69.0
|
1.0
|
|
HD22
|
B:ASN385
|
4.4
|
60.7
|
1.0
|
|
O
|
B:GLY133
|
4.4
|
43.9
|
1.0
|
|
N
|
B:LYS134
|
4.4
|
48.0
|
1.0
|
|
HA
|
B:SER228
|
4.4
|
50.2
|
1.0
|
|
HG3
|
B:LYS367
|
4.5
|
58.0
|
1.0
|
|
C
|
B:GLY133
|
4.5
|
46.7
|
1.0
|
|
CA
|
B:LYS367
|
4.5
|
57.0
|
1.0
|
|
CG
|
B:LYS134
|
4.5
|
58.4
|
1.0
|
|
O
|
B:SER227
|
4.5
|
47.1
|
1.0
|
|
HE1
|
B:PHE369
|
4.6
|
51.5
|
1.0
|
|
HD2
|
B:HIS132
|
4.6
|
49.1
|
1.0
|
|
HZ3
|
B:LYS134
|
4.6
|
0.8
|
1.0
|
|
C04
|
B:EQ8502
|
4.7
|
67.9
|
1.0
|
|
O
|
B:PHE366
|
4.7
|
57.3
|
1.0
|
|
HA
|
B:LYS367
|
4.7
|
62.2
|
1.0
|
|
HD21
|
B:ASN385
|
4.8
|
60.7
|
1.0
|
|
HD2
|
B:LYS367
|
4.8
|
75.4
|
1.0
|
|
CA
|
B:SER228
|
4.8
|
49.5
|
1.0
|
|
HG3
|
B:LYS134
|
4.8
|
70.4
|
1.0
|
|
H
|
B:LYS134
|
4.8
|
49.8
|
1.0
|
|
ND2
|
B:ASN385
|
4.8
|
54.1
|
1.0
|
|
CB
|
B:LYS134
|
4.9
|
54.5
|
1.0
|
|
HA2
|
B:GLY133
|
4.9
|
49.7
|
1.0
|
|
N
|
B:LYS367
|
4.9
|
57.2
|
1.0
|
|
NZ
|
B:LYS367
|
4.9
|
59.8
|
1.0
|
|
OG
|
B:SER228
|
4.9
|
58.4
|
1.0
|
|
HZ2
|
B:LYS134
|
4.9
|
0.8
|
1.0
|
|
C
|
B:PHE366
|
4.9
|
58.5
|
1.0
|
|
HZ3
|
B:LYS367
|
5.0
|
71.3
|
1.0
|
|
C05
|
B:EQ8502
|
5.0
|
75.5
|
1.0
|
|
Reference:
J.Piton,
A.Vocat,
A.Lupien,
C.S.Foo,
O.Riabova,
V.Makarov,
S.T.Cole.
Structure-Based Drug Design and Characterization of Sulfonyl-Piperazine Benzothiazinone Inhibitors of DPRE1 From Mycobacterium Tuberculosis. Antimicrob. Agents V. 62 2018CHEMOTHER..
ISSN: ESSN 1098-6596
PubMed: 30012754
DOI: 10.1128/AAC.00681-18
Page generated: Thu Aug 1 20:24:42 2024
|