Fluorine in PDB 7dia: Falcilysin in Complex with Mefloquine
Protein crystallography data
The structure of Falcilysin in Complex with Mefloquine, PDB code: 7dia
was solved by
J.Q.Lin,
A.El Sahili,
J.Lescar,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.77 /
1.55
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
93.46,
105.74,
126.35,
90,
90,
90
|
R / Rfree (%)
|
17.4 /
19.7
|
Other elements in 7dia:
The structure of Falcilysin in Complex with Mefloquine also contains other interesting chemical elements:
Fluorine Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Fluorine atom in the Falcilysin in Complex with Mefloquine
(pdb code 7dia). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 12 binding sites of Fluorine where determined in the
Falcilysin in Complex with Mefloquine, PDB code: 7dia:
Jump to Fluorine binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Fluorine binding site 1 out
of 12 in 7dia
Go back to
Fluorine Binding Sites List in 7dia
Fluorine binding site 1 out
of 12 in the Falcilysin in Complex with Mefloquine
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Falcilysin in Complex with Mefloquine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1201
b:33.7
occ:1.00
|
FAE
|
A:H8O1201
|
0.0
|
33.7
|
1.0
|
CAZ
|
A:H8O1201
|
1.4
|
38.9
|
1.0
|
FAF
|
A:H8O1201
|
2.2
|
37.5
|
1.0
|
FAG
|
A:H8O1201
|
2.2
|
33.0
|
1.0
|
CAT
|
A:H8O1201
|
2.4
|
30.5
|
1.0
|
NAP
|
A:H8O1201
|
2.9
|
30.7
|
1.0
|
CAV
|
A:H8O1201
|
3.0
|
34.6
|
1.0
|
CZ
|
A:PHE82
|
3.4
|
27.8
|
1.0
|
CAI
|
A:H8O1201
|
3.5
|
33.6
|
1.0
|
CE2
|
A:PHE82
|
3.5
|
29.7
|
1.0
|
CE1
|
A:PHE545
|
3.8
|
35.7
|
1.0
|
CE1
|
A:PHE527
|
4.0
|
35.9
|
1.0
|
CB
|
A:ALA517
|
4.0
|
26.3
|
1.0
|
CD2
|
A:LEU514
|
4.0
|
31.4
|
1.0
|
CAR
|
A:H8O1201
|
4.1
|
31.9
|
1.0
|
FAB
|
A:H8O1201
|
4.2
|
48.5
|
1.0
|
CD1
|
A:PHE545
|
4.3
|
38.1
|
1.0
|
CAU
|
A:H8O1201
|
4.3
|
30.7
|
1.0
|
CD1
|
A:PHE527
|
4.4
|
33.5
|
1.0
|
CE1
|
A:PHE82
|
4.4
|
29.2
|
1.0
|
CAH
|
A:H8O1201
|
4.6
|
32.0
|
1.0
|
CD2
|
A:PHE82
|
4.6
|
27.9
|
1.0
|
CAY
|
A:H8O1201
|
4.7
|
41.2
|
1.0
|
CZ
|
A:PHE545
|
4.8
|
27.4
|
1.0
|
CAJ
|
A:H8O1201
|
5.0
|
29.3
|
1.0
|
|
Fluorine binding site 2 out
of 12 in 7dia
Go back to
Fluorine Binding Sites List in 7dia
Fluorine binding site 2 out
of 12 in the Falcilysin in Complex with Mefloquine
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Falcilysin in Complex with Mefloquine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1201
b:37.5
occ:1.00
|
FAF
|
A:H8O1201
|
0.0
|
37.5
|
1.0
|
CAZ
|
A:H8O1201
|
1.4
|
38.9
|
1.0
|
FAG
|
A:H8O1201
|
2.2
|
33.0
|
1.0
|
FAE
|
A:H8O1201
|
2.2
|
33.7
|
1.0
|
CAT
|
A:H8O1201
|
2.4
|
30.5
|
1.0
|
CAI
|
A:H8O1201
|
2.7
|
33.6
|
1.0
|
CE1
|
A:PHE527
|
3.2
|
35.9
|
1.0
|
CB
|
A:ALA517
|
3.5
|
26.3
|
1.0
|
O
|
A:HOH1753
|
3.5
|
31.2
|
1.0
|
CB
|
A:ASP526
|
3.5
|
25.0
|
1.0
|
CD1
|
A:PHE527
|
3.6
|
33.5
|
1.0
|
CAV
|
A:H8O1201
|
3.7
|
34.6
|
1.0
|
CAH
|
A:H8O1201
|
4.0
|
32.0
|
1.0
|
NAP
|
A:H8O1201
|
4.2
|
30.7
|
1.0
|
CG
|
A:ASP526
|
4.3
|
35.8
|
1.0
|
OD2
|
A:ASP526
|
4.3
|
42.9
|
1.0
|
CZ
|
A:PHE527
|
4.3
|
26.2
|
1.0
|
CE2
|
A:PHE82
|
4.4
|
29.7
|
1.0
|
CA
|
A:ALA517
|
4.7
|
23.6
|
1.0
|
N
|
A:PHE527
|
4.7
|
20.0
|
1.0
|
C
|
A:ASP526
|
4.7
|
24.1
|
1.0
|
O
|
A:ALA517
|
4.7
|
28.9
|
1.0
|
O
|
A:LYS523
|
4.7
|
22.9
|
1.0
|
CA
|
A:ASP526
|
4.7
|
25.8
|
1.0
|
CAU
|
A:H8O1201
|
4.8
|
30.7
|
1.0
|
CG
|
A:PHE527
|
4.8
|
23.9
|
1.0
|
C
|
A:ALA517
|
4.9
|
31.7
|
1.0
|
CE1
|
A:PHE545
|
4.9
|
35.7
|
1.0
|
CZ
|
A:PHE82
|
4.9
|
27.8
|
1.0
|
CAJ
|
A:H8O1201
|
4.9
|
29.3
|
1.0
|
|
Fluorine binding site 3 out
of 12 in 7dia
Go back to
Fluorine Binding Sites List in 7dia
Fluorine binding site 3 out
of 12 in the Falcilysin in Complex with Mefloquine
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Falcilysin in Complex with Mefloquine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1201
b:33.0
occ:1.00
|
FAG
|
A:H8O1201
|
0.0
|
33.0
|
1.0
|
CAZ
|
A:H8O1201
|
1.4
|
38.9
|
1.0
|
FAF
|
A:H8O1201
|
2.2
|
37.5
|
1.0
|
FAE
|
A:H8O1201
|
2.2
|
33.7
|
1.0
|
CAT
|
A:H8O1201
|
2.3
|
30.5
|
1.0
|
NAP
|
A:H8O1201
|
2.9
|
30.7
|
1.0
|
CAV
|
A:H8O1201
|
3.0
|
34.6
|
1.0
|
CAI
|
A:H8O1201
|
3.4
|
33.6
|
1.0
|
CD1
|
A:PHE527
|
3.5
|
33.5
|
1.0
|
CE1
|
A:PHE545
|
3.6
|
35.7
|
1.0
|
CG
|
A:GLU530
|
3.7
|
25.1
|
0.5
|
CB
|
A:ASP526
|
3.8
|
25.0
|
1.0
|
O
|
A:ASP526
|
3.8
|
21.2
|
1.0
|
CE1
|
A:PHE527
|
3.8
|
35.9
|
1.0
|
C
|
A:ASP526
|
3.9
|
24.1
|
1.0
|
CZ
|
A:PHE545
|
4.0
|
27.4
|
1.0
|
N
|
A:PHE527
|
4.1
|
20.0
|
1.0
|
CAR
|
A:H8O1201
|
4.1
|
31.9
|
1.0
|
FAB
|
A:H8O1201
|
4.2
|
48.5
|
1.0
|
CA
|
A:PHE527
|
4.3
|
18.4
|
1.0
|
CAU
|
A:H8O1201
|
4.3
|
30.7
|
1.0
|
CB
|
A:GLU530
|
4.4
|
24.8
|
0.5
|
CB
|
A:GLU530
|
4.4
|
24.9
|
0.5
|
CA
|
A:ASP526
|
4.5
|
25.8
|
1.0
|
CAH
|
A:H8O1201
|
4.5
|
32.0
|
1.0
|
CD1
|
A:PHE545
|
4.7
|
38.1
|
1.0
|
CG
|
A:PHE527
|
4.7
|
23.9
|
1.0
|
CAY
|
A:H8O1201
|
4.8
|
41.2
|
1.0
|
CG
|
A:GLU530
|
4.9
|
26.1
|
0.5
|
CD
|
A:GLU530
|
4.9
|
30.2
|
0.5
|
CAJ
|
A:H8O1201
|
4.9
|
29.3
|
1.0
|
CG
|
A:ASP526
|
5.0
|
35.8
|
1.0
|
|
Fluorine binding site 4 out
of 12 in 7dia
Go back to
Fluorine Binding Sites List in 7dia
Fluorine binding site 4 out
of 12 in the Falcilysin in Complex with Mefloquine
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 4 of Falcilysin in Complex with Mefloquine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1201
b:43.5
occ:1.00
|
FAC
|
A:H8O1201
|
0.0
|
43.5
|
1.0
|
CAY
|
A:H8O1201
|
1.4
|
41.2
|
1.0
|
FAB
|
A:H8O1201
|
2.2
|
48.5
|
1.0
|
FAD
|
A:H8O1201
|
2.2
|
41.1
|
1.0
|
CAR
|
A:H8O1201
|
2.4
|
31.9
|
1.0
|
OE2
|
A:GLU530
|
2.7
|
32.9
|
0.5
|
CAK
|
A:H8O1201
|
2.8
|
30.5
|
1.0
|
OE1
|
A:GLU530
|
3.1
|
31.9
|
0.5
|
OH
|
A:TYR413
|
3.1
|
26.7
|
1.0
|
CD
|
A:GLU530
|
3.3
|
33.9
|
0.5
|
CD1
|
A:ILE544
|
3.4
|
47.6
|
1.0
|
NAP
|
A:H8O1201
|
3.4
|
30.7
|
1.0
|
CE2
|
A:TYR413
|
3.5
|
22.6
|
1.0
|
CD
|
A:GLU530
|
3.6
|
30.2
|
0.5
|
CZ
|
A:TYR413
|
3.6
|
27.0
|
1.0
|
CG
|
A:GLU530
|
3.8
|
26.1
|
0.5
|
OE1
|
A:GLU530
|
4.1
|
35.8
|
0.5
|
CAS
|
A:H8O1201
|
4.1
|
30.9
|
1.0
|
CG
|
A:GLU530
|
4.2
|
25.1
|
0.5
|
CG1
|
A:ILE544
|
4.2
|
43.1
|
1.0
|
OE2
|
A:GLU530
|
4.3
|
34.9
|
0.5
|
CAV
|
A:H8O1201
|
4.6
|
34.6
|
1.0
|
O
|
A:HOH1490
|
4.6
|
32.8
|
1.0
|
CD2
|
A:TYR413
|
4.6
|
25.1
|
1.0
|
CB
|
A:ILE544
|
4.7
|
39.4
|
1.0
|
CB
|
A:GLU530
|
4.8
|
24.9
|
0.5
|
CE1
|
A:TYR413
|
4.8
|
24.9
|
1.0
|
OAA
|
A:H8O1201
|
4.8
|
31.6
|
1.0
|
CB
|
A:GLU530
|
4.9
|
24.8
|
0.5
|
CAU
|
A:H8O1201
|
4.9
|
30.7
|
1.0
|
|
Fluorine binding site 5 out
of 12 in 7dia
Go back to
Fluorine Binding Sites List in 7dia
Fluorine binding site 5 out
of 12 in the Falcilysin in Complex with Mefloquine
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 5 of Falcilysin in Complex with Mefloquine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1201
b:41.1
occ:1.00
|
FAD
|
A:H8O1201
|
0.0
|
41.1
|
1.0
|
CAY
|
A:H8O1201
|
1.4
|
41.2
|
1.0
|
FAC
|
A:H8O1201
|
2.2
|
43.5
|
1.0
|
FAB
|
A:H8O1201
|
2.2
|
48.5
|
1.0
|
CAR
|
A:H8O1201
|
2.4
|
31.9
|
1.0
|
CAK
|
A:H8O1201
|
3.0
|
30.5
|
1.0
|
NAP
|
A:H8O1201
|
3.3
|
30.7
|
1.0
|
CE2
|
A:TYR413
|
3.8
|
22.6
|
1.0
|
CD2
|
A:LEU514
|
4.0
|
31.4
|
1.0
|
OH
|
A:TYR413
|
4.2
|
26.7
|
1.0
|
CAS
|
A:H8O1201
|
4.2
|
30.9
|
1.0
|
CD1
|
A:LEU514
|
4.4
|
34.9
|
1.0
|
CAV
|
A:H8O1201
|
4.5
|
34.6
|
1.0
|
CD1
|
A:ILE544
|
4.5
|
47.6
|
1.0
|
CZ
|
A:TYR413
|
4.5
|
27.0
|
1.0
|
CG1
|
A:ILE544
|
4.6
|
43.1
|
1.0
|
CD1
|
A:LEU417
|
4.6
|
22.0
|
1.0
|
CD2
|
A:TYR413
|
4.7
|
25.1
|
1.0
|
O
|
A:ILE544
|
4.8
|
40.1
|
1.0
|
CB
|
A:ILE544
|
4.8
|
39.4
|
1.0
|
CZ
|
A:PHE414
|
4.8
|
25.2
|
1.0
|
CE1
|
A:PHE414
|
4.8
|
26.3
|
1.0
|
CG
|
A:LEU514
|
4.9
|
32.3
|
1.0
|
OE2
|
A:GLU530
|
4.9
|
32.9
|
0.5
|
CAU
|
A:H8O1201
|
4.9
|
30.7
|
1.0
|
|
Fluorine binding site 6 out
of 12 in 7dia
Go back to
Fluorine Binding Sites List in 7dia
Fluorine binding site 6 out
of 12 in the Falcilysin in Complex with Mefloquine
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 6 of Falcilysin in Complex with Mefloquine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1201
b:48.5
occ:1.00
|
FAB
|
A:H8O1201
|
0.0
|
48.5
|
1.0
|
CAY
|
A:H8O1201
|
1.4
|
41.2
|
1.0
|
FAC
|
A:H8O1201
|
2.2
|
43.5
|
1.0
|
FAD
|
A:H8O1201
|
2.2
|
41.1
|
1.0
|
CAR
|
A:H8O1201
|
2.4
|
31.9
|
1.0
|
NAP
|
A:H8O1201
|
2.7
|
30.7
|
1.0
|
CD1
|
A:ILE544
|
3.5
|
47.6
|
1.0
|
CG
|
A:GLU530
|
3.6
|
26.1
|
0.5
|
CAK
|
A:H8O1201
|
3.6
|
30.5
|
1.0
|
CG1
|
A:ILE544
|
3.8
|
43.1
|
1.0
|
OE2
|
A:GLU530
|
3.9
|
32.9
|
0.5
|
CD
|
A:GLU530
|
4.0
|
33.9
|
0.5
|
CAV
|
A:H8O1201
|
4.0
|
34.6
|
1.0
|
CE1
|
A:PHE545
|
4.1
|
35.7
|
1.0
|
CG
|
A:GLU530
|
4.1
|
25.1
|
0.5
|
CZ
|
A:PHE545
|
4.2
|
27.4
|
1.0
|
OE1
|
A:GLU530
|
4.2
|
31.9
|
0.5
|
FAE
|
A:H8O1201
|
4.2
|
33.7
|
1.0
|
FAG
|
A:H8O1201
|
4.2
|
33.0
|
1.0
|
CD1
|
A:PHE545
|
4.2
|
38.1
|
1.0
|
CD
|
A:GLU530
|
4.4
|
30.2
|
0.5
|
CE2
|
A:PHE545
|
4.5
|
29.5
|
1.0
|
CB
|
A:GLU530
|
4.5
|
24.9
|
0.5
|
CB
|
A:GLU530
|
4.5
|
24.8
|
0.5
|
CG
|
A:PHE545
|
4.5
|
29.1
|
1.0
|
CAZ
|
A:H8O1201
|
4.6
|
38.9
|
1.0
|
CD2
|
A:PHE545
|
4.7
|
29.1
|
1.0
|
CB
|
A:ILE544
|
4.7
|
39.4
|
1.0
|
CAS
|
A:H8O1201
|
4.7
|
30.9
|
1.0
|
CAT
|
A:H8O1201
|
4.8
|
30.5
|
1.0
|
N
|
A:PHE545
|
4.8
|
37.5
|
1.0
|
OE1
|
A:GLU530
|
4.9
|
35.8
|
0.5
|
CD2
|
A:LEU514
|
4.9
|
31.4
|
1.0
|
CAU
|
A:H8O1201
|
4.9
|
30.7
|
1.0
|
CA
|
A:PHE545
|
5.0
|
30.8
|
1.0
|
C
|
A:ILE544
|
5.0
|
39.2
|
1.0
|
|
Fluorine binding site 7 out
of 12 in 7dia
Go back to
Fluorine Binding Sites List in 7dia
Fluorine binding site 7 out
of 12 in the Falcilysin in Complex with Mefloquine
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 7 of Falcilysin in Complex with Mefloquine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1204
b:39.9
occ:1.00
|
FAE
|
A:YMZ1204
|
0.0
|
39.9
|
1.0
|
CAZ
|
A:YMZ1204
|
1.4
|
34.6
|
1.0
|
FAF
|
A:YMZ1204
|
2.2
|
34.8
|
1.0
|
FAG
|
A:YMZ1204
|
2.2
|
39.7
|
1.0
|
CAT
|
A:YMZ1204
|
2.4
|
35.0
|
1.0
|
NAP
|
A:YMZ1204
|
3.0
|
41.0
|
1.0
|
CAV
|
A:YMZ1204
|
3.0
|
39.6
|
1.0
|
CE2
|
A:TYR868
|
3.3
|
35.6
|
1.0
|
CAI
|
A:YMZ1204
|
3.4
|
36.5
|
1.0
|
CD2
|
A:TYR868
|
3.4
|
29.5
|
1.0
|
CB
|
A:ALA1066
|
3.4
|
18.8
|
1.0
|
CZ
|
A:TYR868
|
4.1
|
31.7
|
1.0
|
CAR
|
A:YMZ1204
|
4.2
|
46.0
|
1.0
|
CG
|
A:TYR868
|
4.3
|
24.5
|
1.0
|
CAU
|
A:YMZ1204
|
4.3
|
40.5
|
1.0
|
CAH
|
A:YMZ1204
|
4.6
|
38.6
|
1.0
|
FAD
|
A:YMZ1204
|
4.6
|
45.7
|
1.0
|
OH
|
A:TYR868
|
4.7
|
46.6
|
1.0
|
CA
|
A:GLY1050
|
4.8
|
22.0
|
1.0
|
FAB
|
A:YMZ1204
|
4.8
|
50.1
|
1.0
|
CAY
|
A:YMZ1204
|
4.8
|
44.9
|
1.0
|
CA
|
A:ALA1066
|
4.9
|
18.9
|
1.0
|
CE1
|
A:TYR868
|
4.9
|
29.8
|
1.0
|
C
|
A:GLY1050
|
4.9
|
18.9
|
1.0
|
CAJ
|
A:YMZ1204
|
4.9
|
42.0
|
1.0
|
CD1
|
A:TYR868
|
5.0
|
26.3
|
1.0
|
|
Fluorine binding site 8 out
of 12 in 7dia
Go back to
Fluorine Binding Sites List in 7dia
Fluorine binding site 8 out
of 12 in the Falcilysin in Complex with Mefloquine
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 8 of Falcilysin in Complex with Mefloquine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1204
b:34.8
occ:1.00
|
FAF
|
A:YMZ1204
|
0.0
|
34.8
|
1.0
|
CAZ
|
A:YMZ1204
|
1.4
|
34.6
|
1.0
|
FAG
|
A:YMZ1204
|
2.2
|
39.7
|
1.0
|
FAE
|
A:YMZ1204
|
2.2
|
39.9
|
1.0
|
CAT
|
A:YMZ1204
|
2.4
|
35.0
|
1.0
|
CAI
|
A:YMZ1204
|
2.7
|
36.5
|
1.0
|
N
|
A:VAL1051
|
3.1
|
17.8
|
1.0
|
C
|
A:GLY1050
|
3.3
|
18.9
|
1.0
|
C
|
A:VAL1051
|
3.5
|
20.3
|
1.0
|
CA
|
A:VAL1051
|
3.5
|
16.6
|
1.0
|
O
|
A:VAL1051
|
3.6
|
20.2
|
1.0
|
CA
|
A:GLY1050
|
3.7
|
22.0
|
1.0
|
CAV
|
A:YMZ1204
|
3.7
|
39.6
|
1.0
|
CB
|
A:ALA1066
|
3.7
|
18.8
|
1.0
|
O
|
A:GLY1050
|
3.8
|
16.9
|
1.0
|
N
|
A:PHE1052
|
4.0
|
18.5
|
1.0
|
CB
|
A:PHE1052
|
4.0
|
18.0
|
1.0
|
CAH
|
A:YMZ1204
|
4.1
|
38.6
|
1.0
|
O2
|
A:EDO1206
|
4.1
|
36.3
|
1.0
|
NAP
|
A:YMZ1204
|
4.2
|
41.0
|
1.0
|
O
|
A:LEU1064
|
4.5
|
18.8
|
1.0
|
N
|
A:ALA1066
|
4.5
|
17.5
|
1.0
|
CA
|
A:PHE1052
|
4.5
|
18.8
|
1.0
|
N
|
A:GLY1050
|
4.8
|
20.6
|
1.0
|
CA
|
A:ALA1066
|
4.8
|
18.9
|
1.0
|
CAU
|
A:YMZ1204
|
4.8
|
40.5
|
1.0
|
C2
|
A:EDO1206
|
4.9
|
37.9
|
1.0
|
CAJ
|
A:YMZ1204
|
4.9
|
42.0
|
1.0
|
C
|
A:SER1065
|
5.0
|
17.1
|
1.0
|
|
Fluorine binding site 9 out
of 12 in 7dia
Go back to
Fluorine Binding Sites List in 7dia
Fluorine binding site 9 out
of 12 in the Falcilysin in Complex with Mefloquine
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 9 of Falcilysin in Complex with Mefloquine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1204
b:39.7
occ:1.00
|
FAG
|
A:YMZ1204
|
0.0
|
39.7
|
1.0
|
CAZ
|
A:YMZ1204
|
1.4
|
34.6
|
1.0
|
FAF
|
A:YMZ1204
|
2.2
|
34.8
|
1.0
|
FAE
|
A:YMZ1204
|
2.2
|
39.9
|
1.0
|
CAT
|
A:YMZ1204
|
2.4
|
35.0
|
1.0
|
NAP
|
A:YMZ1204
|
2.8
|
41.0
|
1.0
|
CAV
|
A:YMZ1204
|
3.0
|
39.6
|
1.0
|
CD2
|
A:LEU1064
|
3.3
|
17.0
|
1.0
|
CAI
|
A:YMZ1204
|
3.5
|
36.5
|
1.0
|
CD2
|
A:TYR868
|
3.7
|
29.5
|
1.0
|
CB
|
A:PHE1052
|
3.8
|
18.0
|
1.0
|
CG
|
A:LEU1064
|
3.9
|
16.7
|
1.0
|
CAR
|
A:YMZ1204
|
4.0
|
46.0
|
1.0
|
CB
|
A:ALA1066
|
4.1
|
18.8
|
1.0
|
FAB
|
A:YMZ1204
|
4.1
|
50.1
|
1.0
|
CAU
|
A:YMZ1204
|
4.3
|
40.5
|
1.0
|
CE2
|
A:TYR868
|
4.4
|
35.6
|
1.0
|
CG
|
A:TYR868
|
4.4
|
24.5
|
1.0
|
CB
|
A:TYR868
|
4.5
|
21.8
|
1.0
|
CAY
|
A:YMZ1204
|
4.6
|
44.9
|
1.0
|
CAH
|
A:YMZ1204
|
4.6
|
38.6
|
1.0
|
CE
|
A:MET872
|
4.6
|
36.3
|
1.0
|
CB
|
A:LEU1064
|
4.7
|
16.1
|
1.0
|
CG
|
A:PHE1052
|
4.7
|
25.9
|
1.0
|
O
|
A:LEU1064
|
4.7
|
18.8
|
1.0
|
N
|
A:PHE1052
|
4.8
|
18.5
|
1.0
|
C
|
A:VAL1051
|
4.9
|
20.3
|
1.0
|
CA
|
A:PHE1052
|
4.9
|
18.8
|
1.0
|
FAD
|
A:YMZ1204
|
5.0
|
45.7
|
1.0
|
CAJ
|
A:YMZ1204
|
5.0
|
42.0
|
1.0
|
|
Fluorine binding site 10 out
of 12 in 7dia
Go back to
Fluorine Binding Sites List in 7dia
Fluorine binding site 10 out
of 12 in the Falcilysin in Complex with Mefloquine
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 10 of Falcilysin in Complex with Mefloquine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F1204
b:51.2
occ:1.00
|
FAC
|
A:YMZ1204
|
0.0
|
51.2
|
1.0
|
CAY
|
A:YMZ1204
|
1.4
|
44.9
|
1.0
|
FAB
|
A:YMZ1204
|
2.2
|
50.1
|
1.0
|
FAD
|
A:YMZ1204
|
2.2
|
45.7
|
1.0
|
CAR
|
A:YMZ1204
|
2.4
|
46.0
|
1.0
|
CAK
|
A:YMZ1204
|
2.7
|
46.0
|
1.0
|
NAP
|
A:YMZ1204
|
3.6
|
41.0
|
1.0
|
O
|
A:HOH1798
|
3.7
|
45.6
|
1.0
|
CAS
|
A:YMZ1204
|
4.0
|
47.3
|
1.0
|
CE
|
A:MET872
|
4.2
|
36.3
|
1.0
|
CB
|
A:ALA869
|
4.2
|
20.5
|
1.0
|
CA
|
A:ALA869
|
4.3
|
20.3
|
1.0
|
CAV
|
A:YMZ1204
|
4.7
|
39.6
|
1.0
|
CAU
|
A:YMZ1204
|
4.9
|
40.5
|
1.0
|
O
|
A:ALA869
|
4.9
|
21.5
|
1.0
|
CAW
|
A:YMZ1204
|
5.0
|
54.3
|
1.0
|
NAQ
|
A:YMZ1204
|
5.0
|
60.6
|
1.0
|
|
Reference:
J.Q.Lin,
J.Q.Lin,
A.El Sahili,
J.Lescar.
N/A N/A.
Page generated: Fri Aug 2 06:28:09 2024
|