Fluorine in PDB 3n0n: Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
Enzymatic activity of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
All present enzymatic activity of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor:
4.2.1.1;
Protein crystallography data
The structure of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor, PDB code: 3n0n
was solved by
B.S.Avvaru,
J.Wagner,
A.H.Robbins,
R.Mckenna,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
19.97 /
1.50
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
42.359,
41.448,
71.961,
90.00,
104.24,
90.00
|
|
R / Rfree (%)
|
14 /
17.1
|
Other elements in 3n0n:
The structure of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
(pdb code 3n0n). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 10 binding sites of Fluorine where determined in the
Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor, PDB code: 3n0n:
Jump to Fluorine binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Fluorine binding site 1 out
of 10 in 3n0n
Go back to
Fluorine Binding Sites List in 3n0n
Fluorine binding site 1 out
of 10 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
 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 Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F263
b:18.7
occ:0.60
|
F11
|
A:P9B263
|
0.0
|
18.7
|
0.6
|
|
C11
|
A:P9B263
|
1.3
|
20.7
|
0.6
|
|
O8
|
A:P9B263
|
1.7
|
15.0
|
0.4
|
|
C8
|
A:P9B263
|
2.1
|
15.3
|
0.4
|
|
F15
|
A:P9B263
|
2.2
|
22.2
|
0.4
|
|
C12
|
A:P9B263
|
2.3
|
22.4
|
0.6
|
|
C15
|
A:P9B263
|
2.3
|
22.4
|
0.4
|
|
C10
|
A:P9B263
|
2.4
|
20.6
|
0.6
|
|
HN7
|
A:P9B263
|
2.4
|
14.5
|
0.6
|
|
N9
|
A:P9B263
|
2.5
|
18.0
|
0.4
|
|
C10
|
A:P9B263
|
2.5
|
21.1
|
0.4
|
|
F12
|
A:P9B263
|
2.6
|
21.3
|
0.6
|
|
HE2
|
A:PHE131
|
2.7
|
16.0
|
1.0
|
|
N9
|
A:P9B263
|
2.8
|
18.0
|
0.6
|
|
N7
|
A:P9B263
|
2.8
|
12.1
|
0.6
|
|
HG11
|
A:VAL135
|
2.8
|
13.5
|
1.0
|
|
C8
|
A:P9B263
|
3.0
|
15.5
|
0.6
|
|
HZ
|
A:PHE131
|
3.0
|
17.2
|
1.0
|
|
HD11
|
A:LEU198
|
3.1
|
12.4
|
1.0
|
|
HN9
|
A:P9B263
|
3.2
|
21.6
|
0.4
|
|
N7
|
A:P9B263
|
3.2
|
12.9
|
0.4
|
|
C14
|
A:P9B263
|
3.3
|
23.1
|
0.4
|
|
CE2
|
A:PHE131
|
3.4
|
13.3
|
1.0
|
|
HD13
|
A:LEU198
|
3.4
|
12.4
|
1.0
|
|
HN9
|
A:P9B263
|
3.4
|
21.6
|
0.6
|
|
CZ
|
A:PHE131
|
3.5
|
14.4
|
1.0
|
|
C11
|
A:P9B263
|
3.6
|
22.7
|
0.4
|
|
C13
|
A:P9B263
|
3.6
|
24.8
|
0.6
|
|
C15
|
A:P9B263
|
3.6
|
23.4
|
0.6
|
|
CD1
|
A:LEU198
|
3.7
|
10.3
|
1.0
|
|
C4
|
A:P9B263
|
3.8
|
9.8
|
0.6
|
|
CG1
|
A:VAL135
|
3.8
|
11.2
|
1.0
|
|
HN7
|
A:P9B263
|
3.8
|
15.5
|
0.4
|
|
H5
|
A:P9B263
|
3.8
|
13.8
|
0.4
|
|
C4
|
A:P9B263
|
3.9
|
11.8
|
0.4
|
|
O8
|
A:P9B263
|
4.0
|
17.1
|
0.6
|
|
HG21
|
A:VAL135
|
4.0
|
15.1
|
1.0
|
|
F14
|
A:P9B263
|
4.0
|
24.1
|
0.4
|
|
H5
|
A:P9B263
|
4.0
|
12.2
|
0.6
|
|
HG12
|
A:VAL135
|
4.1
|
13.5
|
1.0
|
|
C14
|
A:P9B263
|
4.1
|
24.8
|
0.6
|
|
C5
|
A:P9B263
|
4.2
|
11.5
|
0.4
|
|
C13
|
A:P9B263
|
4.2
|
23.2
|
0.4
|
|
HD2
|
A:PRO202
|
4.2
|
14.0
|
1.0
|
|
HD21
|
A:LEU198
|
4.2
|
11.9
|
1.0
|
|
C5
|
A:P9B263
|
4.2
|
10.2
|
0.6
|
|
C12
|
A:P9B263
|
4.3
|
23.1
|
0.4
|
|
HD12
|
A:LEU198
|
4.3
|
12.4
|
1.0
|
|
HG13
|
A:VAL135
|
4.3
|
13.5
|
1.0
|
|
HB
|
A:VAL135
|
4.3
|
13.4
|
1.0
|
|
F11
|
A:P9B263
|
4.4
|
23.6
|
0.4
|
|
HD22
|
A:LEU198
|
4.4
|
11.9
|
1.0
|
|
O
|
A:HOH347
|
4.4
|
16.8
|
1.0
|
|
CB
|
A:VAL135
|
4.5
|
11.2
|
1.0
|
|
HD12
|
A:LEU204
|
4.6
|
18.9
|
1.0
|
|
HD11
|
A:LEU141
|
4.6
|
5.3
|
0.5
|
|
CD2
|
A:PHE131
|
4.6
|
12.6
|
1.0
|
|
CD2
|
A:LEU198
|
4.7
|
9.9
|
1.0
|
|
C3
|
A:P9B263
|
4.7
|
8.8
|
0.6
|
|
F15
|
A:P9B263
|
4.7
|
24.5
|
0.6
|
|
CG2
|
A:VAL135
|
4.7
|
12.6
|
1.0
|
|
F13
|
A:P9B263
|
4.7
|
26.5
|
0.6
|
|
H3
|
A:P9B263
|
4.8
|
10.5
|
0.6
|
|
HD21
|
A:LEU141
|
4.8
|
22.0
|
0.5
|
|
CE1
|
A:PHE131
|
4.8
|
13.7
|
1.0
|
|
CG
|
A:LEU198
|
4.8
|
7.4
|
1.0
|
|
HD2
|
A:PHE131
|
4.9
|
15.1
|
1.0
|
|
CD
|
A:PRO202
|
4.9
|
11.7
|
1.0
|
|
HG2
|
A:PRO202
|
5.0
|
15.9
|
1.0
|
|
Fluorine binding site 2 out
of 10 in 3n0n
Go back to
Fluorine Binding Sites List in 3n0n
Fluorine binding site 2 out
of 10 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
 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 Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F263
b:23.6
occ:0.40
|
F11
|
A:P9B263
|
0.0
|
23.6
|
0.4
|
|
HN9
|
A:P9B263
|
1.1
|
21.6
|
0.6
|
|
C11
|
A:P9B263
|
1.3
|
22.7
|
0.4
|
|
N9
|
A:P9B263
|
1.9
|
18.0
|
0.6
|
|
C12
|
A:P9B263
|
2.4
|
23.1
|
0.4
|
|
C10
|
A:P9B263
|
2.4
|
21.1
|
0.4
|
|
F15
|
A:P9B263
|
2.4
|
24.5
|
0.6
|
|
C10
|
A:P9B263
|
2.6
|
20.6
|
0.6
|
|
F12
|
A:P9B263
|
2.7
|
23.7
|
0.4
|
|
N9
|
A:P9B263
|
2.8
|
18.0
|
0.4
|
|
C15
|
A:P9B263
|
2.8
|
23.4
|
0.6
|
|
C8
|
A:P9B263
|
3.1
|
15.5
|
0.6
|
|
HN9
|
A:P9B263
|
3.2
|
21.6
|
0.4
|
|
O
|
A:HOH531
|
3.3
|
25.8
|
1.0
|
|
O8
|
A:P9B263
|
3.4
|
17.1
|
0.6
|
|
C8
|
A:P9B263
|
3.5
|
15.3
|
0.4
|
|
HE2
|
A:PHE131
|
3.5
|
16.0
|
1.0
|
|
O
|
A:HOH412
|
3.5
|
33.8
|
1.0
|
|
C15
|
A:P9B263
|
3.6
|
22.4
|
0.4
|
|
C13
|
A:P9B263
|
3.6
|
23.2
|
0.4
|
|
O8
|
A:P9B263
|
3.7
|
15.0
|
0.4
|
|
C11
|
A:P9B263
|
3.8
|
20.7
|
0.6
|
|
C14
|
A:P9B263
|
4.1
|
24.8
|
0.6
|
|
C14
|
A:P9B263
|
4.1
|
23.1
|
0.4
|
|
CE2
|
A:PHE131
|
4.2
|
13.3
|
1.0
|
|
N7
|
A:P9B263
|
4.3
|
12.1
|
0.6
|
|
F11
|
A:P9B263
|
4.4
|
18.7
|
0.6
|
|
HN7
|
A:P9B263
|
4.4
|
14.5
|
0.6
|
|
N7
|
A:P9B263
|
4.5
|
12.9
|
0.4
|
|
HN7
|
A:P9B263
|
4.7
|
15.5
|
0.4
|
|
F13
|
A:P9B263
|
4.7
|
23.5
|
0.4
|
|
F15
|
A:P9B263
|
4.7
|
22.2
|
0.4
|
|
HD2
|
A:PHE131
|
4.8
|
15.1
|
1.0
|
|
C12
|
A:P9B263
|
4.8
|
22.4
|
0.6
|
|
F14
|
A:P9B263
|
4.8
|
25.4
|
0.6
|
|
CD2
|
A:PHE131
|
4.9
|
12.6
|
1.0
|
|
HZ
|
A:PHE131
|
4.9
|
17.2
|
1.0
|
|
C13
|
A:P9B263
|
5.0
|
24.8
|
0.6
|
|
CZ
|
A:PHE131
|
5.0
|
14.4
|
1.0
|
|
Fluorine binding site 3 out
of 10 in 3n0n
Go back to
Fluorine Binding Sites List in 3n0n
Fluorine binding site 3 out
of 10 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
 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 Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F263
b:21.3
occ:0.60
|
F12
|
A:P9B263
|
0.0
|
21.3
|
0.6
|
|
F15
|
A:P9B263
|
1.3
|
22.2
|
0.4
|
|
C12
|
A:P9B263
|
1.3
|
22.4
|
0.6
|
|
C11
|
A:P9B263
|
2.3
|
20.7
|
0.6
|
|
C13
|
A:P9B263
|
2.4
|
24.8
|
0.6
|
|
C15
|
A:P9B263
|
2.5
|
22.4
|
0.4
|
|
F11
|
A:P9B263
|
2.6
|
18.7
|
0.6
|
|
HD12
|
A:LEU204
|
2.7
|
18.9
|
1.0
|
|
F13
|
A:P9B263
|
2.9
|
26.5
|
0.6
|
|
HG3
|
A:PRO202
|
2.9
|
15.9
|
1.0
|
|
HG21
|
A:VAL135
|
2.9
|
15.1
|
1.0
|
|
HG2
|
A:PRO202
|
3.0
|
15.9
|
1.0
|
|
F14
|
A:P9B263
|
3.0
|
24.1
|
0.4
|
|
C14
|
A:P9B263
|
3.2
|
23.1
|
0.4
|
|
HD11
|
A:LEU198
|
3.2
|
12.4
|
1.0
|
|
CG
|
A:PRO202
|
3.3
|
13.2
|
1.0
|
|
HD11
|
A:LEU204
|
3.3
|
18.9
|
1.0
|
|
HD2
|
A:PRO202
|
3.3
|
14.0
|
1.0
|
|
CD1
|
A:LEU204
|
3.4
|
15.8
|
1.0
|
|
HG11
|
A:VAL135
|
3.6
|
13.5
|
1.0
|
|
C10
|
A:P9B263
|
3.6
|
20.6
|
0.6
|
|
C10
|
A:P9B263
|
3.6
|
21.1
|
0.4
|
|
C14
|
A:P9B263
|
3.6
|
24.8
|
0.6
|
|
CD
|
A:PRO202
|
3.7
|
11.7
|
1.0
|
|
HB
|
A:VAL135
|
3.7
|
13.4
|
1.0
|
|
N9
|
A:P9B263
|
3.8
|
18.0
|
0.4
|
|
CG2
|
A:VAL135
|
3.8
|
12.6
|
1.0
|
|
CD1
|
A:LEU198
|
3.8
|
10.3
|
1.0
|
|
HD12
|
A:LEU198
|
3.8
|
12.4
|
1.0
|
|
HD3
|
A:PRO202
|
3.8
|
14.0
|
1.0
|
|
HD13
|
A:LEU198
|
3.8
|
12.4
|
1.0
|
|
HN7
|
A:P9B263
|
4.0
|
14.5
|
0.6
|
|
HD13
|
A:LEU204
|
4.1
|
18.9
|
1.0
|
|
HG23
|
A:VAL135
|
4.1
|
15.1
|
1.0
|
|
C15
|
A:P9B263
|
4.1
|
23.4
|
0.6
|
|
HN9
|
A:P9B263
|
4.1
|
21.6
|
0.4
|
|
CB
|
A:VAL135
|
4.1
|
11.2
|
1.0
|
|
C8
|
A:P9B263
|
4.1
|
15.3
|
0.4
|
|
HG
|
A:LEU204
|
4.2
|
15.5
|
1.0
|
|
O8
|
A:P9B263
|
4.2
|
15.0
|
0.4
|
|
CG1
|
A:VAL135
|
4.3
|
11.2
|
1.0
|
|
O
|
A:HOH301
|
4.4
|
46.1
|
1.0
|
|
CG
|
A:LEU204
|
4.4
|
12.9
|
1.0
|
|
HG22
|
A:VAL135
|
4.5
|
15.1
|
1.0
|
|
C13
|
A:P9B263
|
4.5
|
23.2
|
0.4
|
|
HE2
|
A:PHE131
|
4.6
|
16.0
|
1.0
|
|
HB2
|
A:LEU204
|
4.7
|
13.8
|
1.0
|
|
CB
|
A:PRO202
|
4.7
|
11.4
|
1.0
|
|
N9
|
A:P9B263
|
4.7
|
18.0
|
0.6
|
|
F14
|
A:P9B263
|
4.7
|
25.4
|
0.6
|
|
HG12
|
A:VAL135
|
4.8
|
13.5
|
1.0
|
|
N7
|
A:P9B263
|
4.8
|
12.1
|
0.6
|
|
C11
|
A:P9B263
|
4.8
|
22.7
|
0.4
|
|
O
|
A:HOH347
|
4.9
|
16.8
|
1.0
|
|
N7
|
A:P9B263
|
4.9
|
12.9
|
0.4
|
|
HG13
|
A:VAL135
|
5.0
|
13.5
|
1.0
|
|
HB2
|
A:PRO202
|
5.0
|
13.7
|
1.0
|
|
Fluorine binding site 4 out
of 10 in 3n0n
Go back to
Fluorine Binding Sites List in 3n0n
Fluorine binding site 4 out
of 10 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
 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 Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F263
b:23.7
occ:0.40
|
F12
|
A:P9B263
|
0.0
|
23.7
|
0.4
|
|
C12
|
A:P9B263
|
1.3
|
23.1
|
0.4
|
|
C11
|
A:P9B263
|
2.3
|
22.7
|
0.4
|
|
C13
|
A:P9B263
|
2.3
|
23.2
|
0.4
|
|
F11
|
A:P9B263
|
2.7
|
23.6
|
0.4
|
|
F13
|
A:P9B263
|
2.7
|
23.5
|
0.4
|
|
HD2
|
A:PHE131
|
3.4
|
15.1
|
1.0
|
|
HN9
|
A:P9B263
|
3.4
|
21.6
|
0.6
|
|
C10
|
A:P9B263
|
3.6
|
21.1
|
0.4
|
|
C14
|
A:P9B263
|
3.6
|
23.1
|
0.4
|
|
HE2
|
A:PHE131
|
3.6
|
16.0
|
1.0
|
|
CD2
|
A:PHE131
|
4.0
|
12.6
|
1.0
|
|
C15
|
A:P9B263
|
4.1
|
22.4
|
0.4
|
|
CE2
|
A:PHE131
|
4.1
|
13.3
|
1.0
|
|
N9
|
A:P9B263
|
4.1
|
18.0
|
0.6
|
|
F15
|
A:P9B263
|
4.3
|
24.5
|
0.6
|
|
C10
|
A:P9B263
|
4.3
|
20.6
|
0.6
|
|
C15
|
A:P9B263
|
4.3
|
23.4
|
0.6
|
|
F14
|
A:P9B263
|
4.7
|
24.1
|
0.4
|
|
N9
|
A:P9B263
|
4.8
|
18.0
|
0.4
|
|
C11
|
A:P9B263
|
5.0
|
20.7
|
0.6
|
|
Fluorine binding site 5 out
of 10 in 3n0n
Go back to
Fluorine Binding Sites List in 3n0n
Fluorine binding site 5 out
of 10 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
 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 Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F263
b:26.5
occ:0.60
|
F13
|
A:P9B263
|
0.0
|
26.5
|
0.6
|
|
C13
|
A:P9B263
|
1.3
|
24.8
|
0.6
|
|
C14
|
A:P9B263
|
2.4
|
24.8
|
0.6
|
|
HG3
|
A:PRO202
|
2.4
|
15.9
|
1.0
|
|
C12
|
A:P9B263
|
2.4
|
22.4
|
0.6
|
|
F15
|
A:P9B263
|
2.6
|
22.2
|
0.4
|
|
F14
|
A:P9B263
|
2.7
|
25.4
|
0.6
|
|
F12
|
A:P9B263
|
2.9
|
21.3
|
0.6
|
|
HD3
|
A:PRO202
|
3.2
|
14.0
|
1.0
|
|
C15
|
A:P9B263
|
3.2
|
22.4
|
0.4
|
|
CG
|
A:PRO202
|
3.3
|
13.2
|
1.0
|
|
O
|
A:HOH301
|
3.3
|
46.1
|
1.0
|
|
F14
|
A:P9B263
|
3.6
|
24.1
|
0.4
|
|
CD
|
A:PRO202
|
3.6
|
11.7
|
1.0
|
|
C15
|
A:P9B263
|
3.6
|
23.4
|
0.6
|
|
C11
|
A:P9B263
|
3.7
|
20.7
|
0.6
|
|
C14
|
A:P9B263
|
3.7
|
23.1
|
0.4
|
|
HG2
|
A:PRO202
|
3.8
|
15.9
|
1.0
|
|
HD2
|
A:PRO202
|
4.0
|
14.0
|
1.0
|
|
HB3
|
A:PRO202
|
4.0
|
13.7
|
1.0
|
|
C10
|
A:P9B263
|
4.1
|
21.1
|
0.4
|
|
C10
|
A:P9B263
|
4.1
|
20.6
|
0.6
|
|
HN9
|
A:P9B263
|
4.2
|
21.6
|
0.4
|
|
CB
|
A:PRO202
|
4.2
|
11.4
|
1.0
|
|
HD11
|
A:LEU204
|
4.4
|
18.9
|
1.0
|
|
N9
|
A:P9B263
|
4.4
|
18.0
|
0.4
|
|
F11
|
A:P9B263
|
4.7
|
18.7
|
0.6
|
|
F15
|
A:P9B263
|
4.7
|
24.5
|
0.6
|
|
HB2
|
A:PRO202
|
4.8
|
13.7
|
1.0
|
|
HD12
|
A:LEU204
|
4.8
|
18.9
|
1.0
|
|
C13
|
A:P9B263
|
4.8
|
23.2
|
0.4
|
|
O
|
A:HOH347
|
4.9
|
16.8
|
1.0
|
|
HG21
|
A:VAL135
|
4.9
|
15.1
|
1.0
|
|
N
|
A:PRO202
|
4.9
|
10.7
|
1.0
|
|
Fluorine binding site 6 out
of 10 in 3n0n
Go back to
Fluorine Binding Sites List in 3n0n
Fluorine binding site 6 out
of 10 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
 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 Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F263
b:23.5
occ:0.40
|
F13
|
A:P9B263
|
0.0
|
23.5
|
0.4
|
|
C13
|
A:P9B263
|
1.3
|
23.2
|
0.4
|
|
C14
|
A:P9B263
|
2.3
|
23.1
|
0.4
|
|
C12
|
A:P9B263
|
2.4
|
23.1
|
0.4
|
|
F14
|
A:P9B263
|
2.7
|
24.1
|
0.4
|
|
F12
|
A:P9B263
|
2.7
|
23.7
|
0.4
|
|
HA2
|
A:GLY132
|
3.0
|
11.8
|
1.0
|
|
HD2
|
A:PHE131
|
3.2
|
15.1
|
1.0
|
|
HA3
|
A:GLY132
|
3.4
|
11.8
|
1.0
|
|
C15
|
A:P9B263
|
3.6
|
22.4
|
0.4
|
|
C11
|
A:P9B263
|
3.6
|
22.7
|
0.4
|
|
CA
|
A:GLY132
|
3.7
|
9.9
|
1.0
|
|
HE2
|
A:PHE131
|
3.9
|
16.0
|
1.0
|
|
CD2
|
A:PHE131
|
4.0
|
12.6
|
1.0
|
|
C10
|
A:P9B263
|
4.1
|
21.1
|
0.4
|
|
N
|
A:GLY132
|
4.2
|
10.4
|
1.0
|
|
H
|
A:GLY132
|
4.3
|
12.5
|
1.0
|
|
O
|
A:HOH474
|
4.3
|
30.2
|
1.0
|
|
CE2
|
A:PHE131
|
4.4
|
13.3
|
1.0
|
|
O
|
A:HOH435
|
4.5
|
25.2
|
1.0
|
|
HG21
|
A:VAL135
|
4.6
|
15.1
|
1.0
|
|
F15
|
A:P9B263
|
4.7
|
22.2
|
0.4
|
|
F11
|
A:P9B263
|
4.7
|
23.6
|
0.4
|
|
HG22
|
A:VAL135
|
4.8
|
15.1
|
1.0
|
|
C11
|
A:P9B263
|
4.9
|
20.7
|
0.6
|
|
C
|
A:PHE131
|
4.9
|
10.2
|
1.0
|
|
HB3
|
A:PHE131
|
4.9
|
12.1
|
1.0
|
|
C12
|
A:P9B263
|
4.9
|
22.4
|
0.6
|
|
C10
|
A:P9B263
|
4.9
|
20.6
|
0.6
|
|
C
|
A:GLY132
|
5.0
|
9.6
|
1.0
|
|
C15
|
A:P9B263
|
5.0
|
23.4
|
0.6
|
|
Fluorine binding site 7 out
of 10 in 3n0n
Go back to
Fluorine Binding Sites List in 3n0n
Fluorine binding site 7 out
of 10 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
 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 Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F263
b:25.4
occ:0.60
|
F14
|
A:P9B263
|
0.0
|
25.4
|
0.6
|
|
C14
|
A:P9B263
|
1.3
|
24.8
|
0.6
|
|
C15
|
A:P9B263
|
2.3
|
23.4
|
0.6
|
|
C13
|
A:P9B263
|
2.3
|
24.8
|
0.6
|
|
F13
|
A:P9B263
|
2.7
|
26.5
|
0.6
|
|
F15
|
A:P9B263
|
2.8
|
24.5
|
0.6
|
|
HN9
|
A:P9B263
|
3.3
|
21.6
|
0.4
|
|
C10
|
A:P9B263
|
3.6
|
20.6
|
0.6
|
|
C12
|
A:P9B263
|
3.6
|
22.4
|
0.6
|
|
C10
|
A:P9B263
|
3.6
|
21.1
|
0.4
|
|
C15
|
A:P9B263
|
3.6
|
22.4
|
0.4
|
|
N9
|
A:P9B263
|
3.8
|
18.0
|
0.4
|
|
F15
|
A:P9B263
|
3.8
|
22.2
|
0.4
|
|
C11
|
A:P9B263
|
4.1
|
20.7
|
0.6
|
|
HD3
|
A:PRO202
|
4.1
|
14.0
|
1.0
|
|
C11
|
A:P9B263
|
4.2
|
22.7
|
0.4
|
|
C14
|
A:P9B263
|
4.2
|
23.1
|
0.4
|
|
O
|
A:HOH347
|
4.3
|
16.8
|
1.0
|
|
HG3
|
A:PRO202
|
4.7
|
15.9
|
1.0
|
|
C12
|
A:P9B263
|
4.7
|
23.1
|
0.4
|
|
C13
|
A:P9B263
|
4.7
|
23.2
|
0.4
|
|
F12
|
A:P9B263
|
4.7
|
21.3
|
0.6
|
|
N9
|
A:P9B263
|
4.8
|
18.0
|
0.6
|
|
F14
|
A:P9B263
|
4.8
|
24.1
|
0.4
|
|
F11
|
A:P9B263
|
4.8
|
23.6
|
0.4
|
|
O
|
A:HOH494
|
4.8
|
34.8
|
1.0
|
|
CD
|
A:PRO202
|
4.9
|
11.7
|
1.0
|
|
HN9
|
A:P9B263
|
5.0
|
21.6
|
0.6
|
|
Fluorine binding site 8 out
of 10 in 3n0n
Go back to
Fluorine Binding Sites List in 3n0n
Fluorine binding site 8 out
of 10 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
 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 Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F263
b:24.1
occ:0.40
|
F14
|
A:P9B263
|
0.0
|
24.1
|
0.4
|
|
C14
|
A:P9B263
|
1.3
|
23.1
|
0.4
|
|
C15
|
A:P9B263
|
2.3
|
22.4
|
0.4
|
|
C13
|
A:P9B263
|
2.3
|
23.2
|
0.4
|
|
HG21
|
A:VAL135
|
2.5
|
15.1
|
1.0
|
|
F13
|
A:P9B263
|
2.7
|
23.5
|
0.4
|
|
F15
|
A:P9B263
|
2.7
|
22.2
|
0.4
|
|
C12
|
A:P9B263
|
3.0
|
22.4
|
0.6
|
|
F12
|
A:P9B263
|
3.0
|
21.3
|
0.6
|
|
O
|
A:HOH435
|
3.2
|
25.2
|
1.0
|
|
C13
|
A:P9B263
|
3.3
|
24.8
|
0.6
|
|
CG2
|
A:VAL135
|
3.3
|
12.6
|
1.0
|
|
HG22
|
A:VAL135
|
3.4
|
15.1
|
1.0
|
|
HA2
|
A:GLY132
|
3.4
|
11.8
|
1.0
|
|
C11
|
A:P9B263
|
3.5
|
20.7
|
0.6
|
|
F13
|
A:P9B263
|
3.6
|
26.5
|
0.6
|
|
C12
|
A:P9B263
|
3.6
|
23.1
|
0.4
|
|
C10
|
A:P9B263
|
3.6
|
21.1
|
0.4
|
|
HG23
|
A:VAL135
|
3.7
|
15.1
|
1.0
|
|
F11
|
A:P9B263
|
4.0
|
18.7
|
0.6
|
|
HG11
|
A:VAL135
|
4.0
|
13.5
|
1.0
|
|
C14
|
A:P9B263
|
4.0
|
24.8
|
0.6
|
|
HE2
|
A:PHE131
|
4.0
|
16.0
|
1.0
|
|
C11
|
A:P9B263
|
4.1
|
22.7
|
0.4
|
|
C10
|
A:P9B263
|
4.2
|
20.6
|
0.6
|
|
CA
|
A:GLY132
|
4.3
|
9.9
|
1.0
|
|
C15
|
A:P9B263
|
4.4
|
23.4
|
0.6
|
|
CB
|
A:VAL135
|
4.5
|
11.2
|
1.0
|
|
HA3
|
A:GLY132
|
4.5
|
11.8
|
1.0
|
|
HD2
|
A:PHE131
|
4.5
|
15.1
|
1.0
|
|
CG1
|
A:VAL135
|
4.6
|
11.2
|
1.0
|
|
O
|
A:GLY132
|
4.6
|
12.7
|
1.0
|
|
CE2
|
A:PHE131
|
4.7
|
13.3
|
1.0
|
|
F12
|
A:P9B263
|
4.7
|
23.7
|
0.4
|
|
HB
|
A:VAL135
|
4.7
|
13.4
|
1.0
|
|
HG13
|
A:VAL135
|
4.7
|
13.5
|
1.0
|
|
N9
|
A:P9B263
|
4.7
|
18.0
|
0.4
|
|
HD12
|
A:LEU204
|
4.8
|
18.9
|
1.0
|
|
F14
|
A:P9B263
|
4.8
|
25.4
|
0.6
|
|
HD11
|
A:LEU204
|
4.8
|
18.9
|
1.0
|
|
O
|
A:HOH301
|
4.9
|
46.1
|
1.0
|
|
CD2
|
A:PHE131
|
4.9
|
12.6
|
1.0
|
|
Fluorine binding site 9 out
of 10 in 3n0n
Go back to
Fluorine Binding Sites List in 3n0n
Fluorine binding site 9 out
of 10 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
 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 Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F263
b:24.5
occ:0.60
|
F15
|
A:P9B263
|
0.0
|
24.5
|
0.6
|
|
C15
|
A:P9B263
|
1.3
|
23.4
|
0.6
|
|
HN9
|
A:P9B263
|
2.0
|
21.6
|
0.4
|
|
C10
|
A:P9B263
|
2.3
|
20.6
|
0.6
|
|
N9
|
A:P9B263
|
2.4
|
18.0
|
0.4
|
|
C14
|
A:P9B263
|
2.4
|
24.8
|
0.6
|
|
F11
|
A:P9B263
|
2.4
|
23.6
|
0.4
|
|
C10
|
A:P9B263
|
2.5
|
21.1
|
0.4
|
|
C11
|
A:P9B263
|
2.5
|
22.7
|
0.4
|
|
N9
|
A:P9B263
|
2.7
|
18.0
|
0.6
|
|
HN9
|
A:P9B263
|
2.7
|
21.6
|
0.6
|
|
F14
|
A:P9B263
|
2.8
|
25.4
|
0.6
|
|
C15
|
A:P9B263
|
3.5
|
22.4
|
0.4
|
|
C12
|
A:P9B263
|
3.6
|
23.1
|
0.4
|
|
C11
|
A:P9B263
|
3.6
|
20.7
|
0.6
|
|
O
|
A:HOH531
|
3.6
|
25.8
|
1.0
|
|
C8
|
A:P9B263
|
3.6
|
15.3
|
0.4
|
|
C13
|
A:P9B263
|
3.7
|
24.8
|
0.6
|
|
O
|
A:HOH347
|
3.8
|
16.8
|
1.0
|
|
C8
|
A:P9B263
|
3.8
|
15.5
|
0.6
|
|
HN7
|
A:P9B263
|
4.0
|
15.5
|
0.4
|
|
O
|
A:HOH384
|
4.0
|
23.1
|
1.0
|
|
C12
|
A:P9B263
|
4.1
|
22.4
|
0.6
|
|
HN7
|
A:P9B263
|
4.1
|
14.5
|
0.6
|
|
F15
|
A:P9B263
|
4.2
|
22.2
|
0.4
|
|
F12
|
A:P9B263
|
4.3
|
23.7
|
0.4
|
|
N7
|
A:P9B263
|
4.3
|
12.9
|
0.4
|
|
C14
|
A:P9B263
|
4.3
|
23.1
|
0.4
|
|
C13
|
A:P9B263
|
4.4
|
23.2
|
0.4
|
|
N7
|
A:P9B263
|
4.4
|
12.1
|
0.6
|
|
O8
|
A:P9B263
|
4.5
|
15.0
|
0.4
|
|
O8
|
A:P9B263
|
4.6
|
17.1
|
0.6
|
|
F11
|
A:P9B263
|
4.7
|
18.7
|
0.6
|
|
F13
|
A:P9B263
|
4.7
|
26.5
|
0.6
|
|
Fluorine binding site 10 out
of 10 in 3n0n
Go back to
Fluorine Binding Sites List in 3n0n
Fluorine binding site 10 out
of 10 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor
 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 Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Inhibitor within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F263
b:22.2
occ:0.40
|
F15
|
A:P9B263
|
0.0
|
22.2
|
0.4
|
|
C12
|
A:P9B263
|
0.4
|
22.4
|
0.6
|
|
F12
|
A:P9B263
|
1.3
|
21.3
|
0.6
|
|
C11
|
A:P9B263
|
1.3
|
20.7
|
0.6
|
|
C15
|
A:P9B263
|
1.3
|
22.4
|
0.4
|
|
C13
|
A:P9B263
|
1.6
|
24.8
|
0.6
|
|
F11
|
A:P9B263
|
2.2
|
18.7
|
0.6
|
|
C14
|
A:P9B263
|
2.3
|
23.1
|
0.4
|
|
C10
|
A:P9B263
|
2.4
|
21.1
|
0.4
|
|
C10
|
A:P9B263
|
2.4
|
20.6
|
0.6
|
|
C14
|
A:P9B263
|
2.6
|
24.8
|
0.6
|
|
F13
|
A:P9B263
|
2.6
|
26.5
|
0.6
|
|
F14
|
A:P9B263
|
2.7
|
24.1
|
0.4
|
|
N9
|
A:P9B263
|
2.7
|
18.0
|
0.4
|
|
C15
|
A:P9B263
|
2.9
|
23.4
|
0.6
|
|
HN9
|
A:P9B263
|
3.1
|
21.6
|
0.4
|
|
C8
|
A:P9B263
|
3.4
|
15.3
|
0.4
|
|
HG3
|
A:PRO202
|
3.4
|
15.9
|
1.0
|
|
HG21
|
A:VAL135
|
3.5
|
15.1
|
1.0
|
|
HN7
|
A:P9B263
|
3.5
|
14.5
|
0.6
|
|
C13
|
A:P9B263
|
3.6
|
23.2
|
0.4
|
|
O8
|
A:P9B263
|
3.6
|
15.0
|
0.4
|
|
HD2
|
A:PRO202
|
3.6
|
14.0
|
1.0
|
|
C11
|
A:P9B263
|
3.6
|
22.7
|
0.4
|
|
N9
|
A:P9B263
|
3.7
|
18.0
|
0.6
|
|
F14
|
A:P9B263
|
3.8
|
25.4
|
0.6
|
|
HD3
|
A:PRO202
|
3.8
|
14.0
|
1.0
|
|
HG11
|
A:VAL135
|
3.8
|
13.5
|
1.0
|
|
HE2
|
A:PHE131
|
3.9
|
16.0
|
1.0
|
|
HG2
|
A:PRO202
|
3.9
|
15.9
|
1.0
|
|
CG
|
A:PRO202
|
3.9
|
13.2
|
1.0
|
|
HD12
|
A:LEU204
|
4.0
|
18.9
|
1.0
|
|
HD11
|
A:LEU198
|
4.0
|
12.4
|
1.0
|
|
CD
|
A:PRO202
|
4.0
|
11.7
|
1.0
|
|
C12
|
A:P9B263
|
4.1
|
23.1
|
0.4
|
|
HN9
|
A:P9B263
|
4.2
|
21.6
|
0.6
|
|
F15
|
A:P9B263
|
4.2
|
24.5
|
0.6
|
|
N7
|
A:P9B263
|
4.2
|
12.1
|
0.6
|
|
HD13
|
A:LEU198
|
4.3
|
12.4
|
1.0
|
|
O
|
A:HOH347
|
4.3
|
16.8
|
1.0
|
|
N7
|
A:P9B263
|
4.4
|
12.9
|
0.4
|
|
CG2
|
A:VAL135
|
4.4
|
12.6
|
1.0
|
|
C8
|
A:P9B263
|
4.4
|
15.5
|
0.6
|
|
HD11
|
A:LEU204
|
4.4
|
18.9
|
1.0
|
|
CD1
|
A:LEU198
|
4.5
|
10.3
|
1.0
|
|
HN7
|
A:P9B263
|
4.5
|
15.5
|
0.4
|
|
HB
|
A:VAL135
|
4.6
|
13.4
|
1.0
|
|
HD12
|
A:LEU198
|
4.6
|
12.4
|
1.0
|
|
CD1
|
A:LEU204
|
4.7
|
15.8
|
1.0
|
|
F13
|
A:P9B263
|
4.7
|
23.5
|
0.4
|
|
CG1
|
A:VAL135
|
4.7
|
11.2
|
1.0
|
|
CE2
|
A:PHE131
|
4.7
|
13.3
|
1.0
|
|
F11
|
A:P9B263
|
4.7
|
23.6
|
0.4
|
|
HG23
|
A:VAL135
|
4.8
|
15.1
|
1.0
|
|
CB
|
A:VAL135
|
4.8
|
11.2
|
1.0
|
|
HG22
|
A:VAL135
|
4.9
|
15.1
|
1.0
|
|
O
|
A:HOH301
|
5.0
|
46.1
|
1.0
|
|
Reference:
F.Pacchiano,
M.Aggarwal,
B.S.Avvaru,
A.H.Robbins,
A.Scozzafava,
R.Mckenna,
C.T.Supuran.
Selective Hydrophobic Pocket Binding Observed Within the Carbonic Anhydrase II Active Site Accommodate Different 4-Substituted-Ureido-Benzenesulfonamides and Correlate to Inhibitor Potency. Chem.Commun.(Camb.) V. 46 8371 2010.
ISSN: ISSN 1359-7345
PubMed: 20922253
DOI: 10.1039/C0CC02707C
Page generated: Wed Jul 31 20:46:32 2024
|
