Fluorine in PDB 7zej: Crystal Structure of the Human MGC45594 Gene Product in Complex with Celecoxib.
Enzymatic activity of Crystal Structure of the Human MGC45594 Gene Product in Complex with Celecoxib.
All present enzymatic activity of Crystal Structure of the Human MGC45594 Gene Product in Complex with Celecoxib.:
1.3.1.48;
Protein crystallography data
The structure of Crystal Structure of the Human MGC45594 Gene Product in Complex with Celecoxib., PDB code: 7zej
was solved by
N.Shafqat,
W.W.Yue,
L.Koekemoer,
F.Niesen,
E.Ugochukwu,
M.Vollmar,
J.Weigelt,
T.Krojer,
A.Pike,
A.Chaikaud,
F.Von Delft,
C.Arrowsmith,
C.Bountra,
A.Edwards,
U.Opperman,
Structural Genomics Consortium (Sgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
16.76 /
1.79
|
|
Space group
|
P 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
46.83,
51.41,
75.88,
93.86,
91.48,
101.29
|
|
R / Rfree (%)
|
18.5 /
23.4
|
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of the Human MGC45594 Gene Product in Complex with Celecoxib.
(pdb code 7zej). 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 the Human MGC45594 Gene Product in Complex with Celecoxib., PDB code: 7zej:
Jump to Fluorine binding site number:
1;
2;
3;
4;
5;
6;
Fluorine binding site 1 out
of 6 in 7zej
Go back to
Fluorine Binding Sites List in 7zej
Fluorine binding site 1 out
of 6 in the Crystal Structure of the Human MGC45594 Gene Product in Complex with Celecoxib.
 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 the Human MGC45594 Gene Product in Complex with Celecoxib. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F402
b:62.6
occ:1.00
|
F3
|
A:CEL402
|
0.0
|
62.6
|
1.0
|
|
C4
|
A:CEL402
|
1.3
|
60.5
|
1.0
|
|
F1
|
A:CEL402
|
2.1
|
45.7
|
1.0
|
|
F2
|
A:CEL402
|
2.2
|
74.4
|
1.0
|
|
C1
|
A:CEL402
|
2.4
|
67.8
|
1.0
|
|
N1
|
A:CEL402
|
2.7
|
76.4
|
1.0
|
|
HG
|
A:SER68
|
2.8
|
13.9
|
0.0
|
|
OH
|
A:TYR77
|
3.0
|
33.8
|
1.0
|
|
HH
|
A:TYR77
|
3.2
|
22.6
|
0.0
|
|
HE1
|
A:PHE295
|
3.2
|
26.9
|
1.0
|
|
OG
|
A:SER68
|
3.6
|
24.4
|
1.0
|
|
HB2
|
A:SER68
|
3.6
|
21.6
|
1.0
|
|
C2
|
A:CEL402
|
3.7
|
69.3
|
1.0
|
|
C3N
|
A:NAP401
|
3.8
|
21.9
|
1.0
|
|
HO2N
|
A:NAP401
|
3.8
|
16.9
|
0.0
|
|
N2
|
A:CEL402
|
3.9
|
78.2
|
1.0
|
|
CB
|
A:SER68
|
3.9
|
21.2
|
1.0
|
|
HB3
|
A:SER68
|
3.9
|
21.6
|
1.0
|
|
C7N
|
A:NAP401
|
4.0
|
21.3
|
1.0
|
|
HD1
|
A:PHE295
|
4.0
|
25.9
|
1.0
|
|
H2N
|
A:NAP401
|
4.0
|
21.3
|
1.0
|
|
C2N
|
A:NAP401
|
4.0
|
21.0
|
1.0
|
|
O7N
|
A:NAP401
|
4.1
|
19.2
|
1.0
|
|
CE1
|
A:PHE295
|
4.1
|
27.4
|
1.0
|
|
CZ
|
A:TYR77
|
4.2
|
34.6
|
1.0
|
|
O
|
A:HOH573
|
4.3
|
19.1
|
1.0
|
|
C4N
|
A:NAP401
|
4.3
|
22.1
|
1.0
|
|
HC2
|
A:CEL402
|
4.3
|
69.0
|
1.0
|
|
CD1
|
A:PHE295
|
4.5
|
26.0
|
1.0
|
|
C3
|
A:CEL402
|
4.5
|
68.6
|
1.0
|
|
H4N
|
A:NAP401
|
4.5
|
21.9
|
1.0
|
|
HE2
|
A:TYR77
|
4.5
|
34.2
|
1.0
|
|
N7N
|
A:NAP401
|
4.6
|
19.4
|
1.0
|
|
O2D
|
A:NAP401
|
4.6
|
18.4
|
1.0
|
|
H13C
|
A:CEL402
|
4.7
|
79.0
|
1.0
|
|
C12
|
A:CEL402
|
4.7
|
77.4
|
1.0
|
|
N1N
|
A:NAP401
|
4.8
|
21.2
|
1.0
|
|
CE2
|
A:TYR77
|
4.8
|
34.9
|
1.0
|
|
H72N
|
A:NAP401
|
4.9
|
19.9
|
1.0
|
|
C5N
|
A:NAP401
|
4.9
|
21.4
|
1.0
|
|
H71N
|
A:NAP401
|
4.9
|
19.9
|
1.0
|
|
Fluorine binding site 2 out
of 6 in 7zej
Go back to
Fluorine Binding Sites List in 7zej
Fluorine binding site 2 out
of 6 in the Crystal Structure of the Human MGC45594 Gene Product in Complex with Celecoxib.
 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 the Human MGC45594 Gene Product in Complex with Celecoxib. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F402
b:74.4
occ:1.00
|
F2
|
A:CEL402
|
0.0
|
74.4
|
1.0
|
|
C4
|
A:CEL402
|
1.3
|
60.5
|
1.0
|
|
F1
|
A:CEL402
|
2.2
|
45.7
|
1.0
|
|
F3
|
A:CEL402
|
2.2
|
62.6
|
1.0
|
|
C1
|
A:CEL402
|
2.3
|
67.8
|
1.0
|
|
H2N
|
A:NAP401
|
2.5
|
21.3
|
1.0
|
|
C2N
|
A:NAP401
|
2.9
|
21.0
|
1.0
|
|
N1
|
A:CEL402
|
2.9
|
76.4
|
1.0
|
|
N7N
|
A:NAP401
|
3.0
|
19.4
|
1.0
|
|
C7N
|
A:NAP401
|
3.0
|
21.3
|
1.0
|
|
C3N
|
A:NAP401
|
3.1
|
21.9
|
1.0
|
|
H71N
|
A:NAP401
|
3.1
|
19.9
|
1.0
|
|
C2
|
A:CEL402
|
3.3
|
69.3
|
1.0
|
|
H72N
|
A:NAP401
|
3.3
|
19.9
|
1.0
|
|
HO2N
|
A:NAP401
|
3.5
|
16.9
|
0.0
|
|
O
|
A:ILE260
|
3.5
|
16.8
|
1.0
|
|
O7N
|
A:NAP401
|
3.6
|
19.2
|
1.0
|
|
HD1
|
A:PHE295
|
3.7
|
25.9
|
1.0
|
|
HC2
|
A:CEL402
|
3.7
|
69.0
|
1.0
|
|
HG
|
A:SER68
|
3.7
|
13.9
|
0.0
|
|
N2
|
A:CEL402
|
4.0
|
78.2
|
1.0
|
|
N1N
|
A:NAP401
|
4.0
|
21.2
|
1.0
|
|
O2D
|
A:NAP401
|
4.0
|
18.4
|
1.0
|
|
HE1
|
A:PHE295
|
4.2
|
26.9
|
1.0
|
|
C4N
|
A:NAP401
|
4.2
|
22.1
|
1.0
|
|
C3
|
A:CEL402
|
4.2
|
68.6
|
1.0
|
|
H1D
|
A:NAP401
|
4.4
|
19.0
|
1.0
|
|
H13C
|
A:CEL402
|
4.4
|
79.0
|
1.0
|
|
OG
|
A:SER68
|
4.4
|
24.4
|
1.0
|
|
CD1
|
A:PHE295
|
4.5
|
26.0
|
1.0
|
|
C1D
|
A:NAP401
|
4.6
|
18.5
|
1.0
|
|
HA2
|
A:GLY261
|
4.6
|
17.4
|
1.0
|
|
H4N
|
A:NAP401
|
4.6
|
21.9
|
1.0
|
|
HA
|
A:PHE295
|
4.7
|
19.9
|
1.0
|
|
HH
|
A:TYR266
|
4.7
|
4.0
|
0.0
|
|
OH
|
A:TYR266
|
4.7
|
16.4
|
1.0
|
|
CE1
|
A:PHE295
|
4.7
|
27.4
|
1.0
|
|
C
|
A:ILE260
|
4.7
|
16.8
|
1.0
|
|
HA3
|
A:GLY261
|
4.8
|
17.4
|
1.0
|
|
C6N
|
A:NAP401
|
4.9
|
19.9
|
1.0
|
|
C2D
|
A:NAP401
|
4.9
|
18.8
|
1.0
|
|
O
|
A:PHE294
|
4.9
|
15.9
|
1.0
|
|
C5N
|
A:NAP401
|
5.0
|
21.4
|
1.0
|
|
OH
|
A:TYR77
|
5.0
|
33.8
|
1.0
|
|
C12
|
A:CEL402
|
5.0
|
77.4
|
1.0
|
|
Fluorine binding site 3 out
of 6 in 7zej
Go back to
Fluorine Binding Sites List in 7zej
Fluorine binding site 3 out
of 6 in the Crystal Structure of the Human MGC45594 Gene Product in Complex with Celecoxib.
 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 the Human MGC45594 Gene Product in Complex with Celecoxib. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F402
b:45.7
occ:1.00
|
F1
|
A:CEL402
|
0.0
|
45.7
|
1.0
|
|
C4
|
A:CEL402
|
1.3
|
60.5
|
1.0
|
|
HO2N
|
A:NAP401
|
1.8
|
16.9
|
0.0
|
|
F3
|
A:CEL402
|
2.1
|
62.6
|
1.0
|
|
F2
|
A:CEL402
|
2.2
|
74.4
|
1.0
|
|
HG
|
A:SER68
|
2.2
|
13.9
|
0.0
|
|
C1
|
A:CEL402
|
2.5
|
67.8
|
1.0
|
|
O2D
|
A:NAP401
|
2.6
|
18.4
|
1.0
|
|
OG
|
A:SER68
|
2.7
|
24.4
|
1.0
|
|
H2N
|
A:NAP401
|
3.0
|
21.3
|
1.0
|
|
O
|
A:HOH573
|
3.1
|
19.1
|
1.0
|
|
C2N
|
A:NAP401
|
3.1
|
21.0
|
1.0
|
|
HB2
|
A:SER68
|
3.2
|
21.6
|
1.0
|
|
C2
|
A:CEL402
|
3.2
|
69.3
|
1.0
|
|
HC2
|
A:CEL402
|
3.3
|
69.0
|
1.0
|
|
CB
|
A:SER68
|
3.4
|
21.2
|
1.0
|
|
N1N
|
A:NAP401
|
3.5
|
21.2
|
1.0
|
|
C2D
|
A:NAP401
|
3.6
|
18.8
|
1.0
|
|
N1
|
A:CEL402
|
3.6
|
76.4
|
1.0
|
|
C3N
|
A:NAP401
|
3.7
|
21.9
|
1.0
|
|
H2D
|
A:NAP401
|
3.7
|
18.5
|
1.0
|
|
C1D
|
A:NAP401
|
3.9
|
18.5
|
1.0
|
|
HB3
|
A:SER68
|
3.9
|
21.6
|
1.0
|
|
OH
|
A:TYR266
|
4.0
|
16.4
|
1.0
|
|
H1D
|
A:NAP401
|
4.0
|
19.0
|
1.0
|
|
HH
|
A:TYR77
|
4.1
|
22.6
|
0.0
|
|
C6N
|
A:NAP401
|
4.1
|
19.9
|
1.0
|
|
C4N
|
A:NAP401
|
4.3
|
22.1
|
1.0
|
|
OH
|
A:TYR77
|
4.3
|
33.8
|
1.0
|
|
H
|
A:SER68
|
4.3
|
18.7
|
1.0
|
|
C7N
|
A:NAP401
|
4.4
|
21.3
|
1.0
|
|
HH
|
A:TYR266
|
4.4
|
4.0
|
0.0
|
|
C3
|
A:CEL402
|
4.5
|
68.6
|
1.0
|
|
C5N
|
A:NAP401
|
4.5
|
21.4
|
1.0
|
|
HE2
|
A:TYR266
|
4.5
|
16.6
|
1.0
|
|
N2
|
A:CEL402
|
4.5
|
78.2
|
1.0
|
|
HD22
|
A:ASN71
|
4.6
|
20.9
|
1.0
|
|
CA
|
A:SER68
|
4.6
|
20.0
|
1.0
|
|
O
|
A:ILE260
|
4.7
|
16.8
|
1.0
|
|
H6N
|
A:NAP401
|
4.7
|
20.5
|
1.0
|
|
H71N
|
A:NAP401
|
4.7
|
19.9
|
1.0
|
|
N7N
|
A:NAP401
|
4.7
|
19.4
|
1.0
|
|
HO3N
|
A:NAP401
|
4.7
|
19.9
|
0.0
|
|
CZ
|
A:TYR266
|
4.8
|
17.4
|
1.0
|
|
N
|
A:SER68
|
4.8
|
18.3
|
1.0
|
|
HA
|
A:SER68
|
4.9
|
19.6
|
1.0
|
|
H4N
|
A:NAP401
|
4.9
|
21.9
|
1.0
|
|
HA3
|
A:GLY261
|
4.9
|
17.4
|
1.0
|
|
CE2
|
A:TYR266
|
4.9
|
16.4
|
1.0
|
|
HB3
|
A:ALA67
|
4.9
|
17.9
|
1.0
|
|
C3D
|
A:NAP401
|
4.9
|
17.8
|
1.0
|
|
O7N
|
A:NAP401
|
5.0
|
19.2
|
1.0
|
|
Fluorine binding site 4 out
of 6 in 7zej
Go back to
Fluorine Binding Sites List in 7zej
Fluorine binding site 4 out
of 6 in the Crystal Structure of the Human MGC45594 Gene Product in Complex with Celecoxib.
 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 the Human MGC45594 Gene Product in Complex with Celecoxib. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F402
b:40.1
occ:1.00
|
F3
|
B:CEL402
|
0.0
|
40.1
|
1.0
|
|
C4
|
B:CEL402
|
1.3
|
56.4
|
1.0
|
|
HO2N
|
B:NAP401
|
2.1
|
16.4
|
0.0
|
|
F2
|
B:CEL402
|
2.1
|
58.1
|
1.0
|
|
F1
|
B:CEL402
|
2.2
|
64.3
|
1.0
|
|
HG
|
B:SER68
|
2.4
|
12.1
|
0.0
|
|
C1
|
B:CEL402
|
2.5
|
57.2
|
1.0
|
|
HB2
|
B:SER68
|
2.6
|
23.3
|
1.0
|
|
OG
|
B:SER68
|
2.9
|
27.3
|
1.0
|
|
O2D
|
B:NAP401
|
2.9
|
18.1
|
1.0
|
|
O
|
B:HOH571
|
3.1
|
14.9
|
1.0
|
|
CB
|
B:SER68
|
3.2
|
22.6
|
1.0
|
|
C2
|
B:CEL402
|
3.4
|
57.6
|
1.0
|
|
H2N
|
B:NAP401
|
3.4
|
17.2
|
1.0
|
|
N1
|
B:CEL402
|
3.5
|
61.0
|
1.0
|
|
C2N
|
B:NAP401
|
3.5
|
16.7
|
1.0
|
|
HB3
|
B:SER68
|
3.7
|
23.3
|
1.0
|
|
HC2
|
B:CEL402
|
3.7
|
57.5
|
1.0
|
|
HH
|
B:TYR77
|
3.9
|
21.9
|
0.0
|
|
C2D
|
B:NAP401
|
3.9
|
18.4
|
1.0
|
|
N1N
|
B:NAP401
|
3.9
|
17.2
|
1.0
|
|
C3N
|
B:NAP401
|
4.0
|
17.8
|
1.0
|
|
H2D
|
B:NAP401
|
4.0
|
18.4
|
1.0
|
|
OH
|
B:TYR77
|
4.1
|
40.1
|
1.0
|
|
H
|
B:SER68
|
4.2
|
19.4
|
1.0
|
|
OH
|
B:TYR266
|
4.2
|
19.3
|
1.0
|
|
C1D
|
B:NAP401
|
4.4
|
18.2
|
1.0
|
|
CA
|
B:SER68
|
4.4
|
21.4
|
1.0
|
|
HE2
|
B:TYR266
|
4.4
|
18.9
|
1.0
|
|
HD22
|
B:ASN71
|
4.5
|
24.0
|
1.0
|
|
C6N
|
B:NAP401
|
4.5
|
17.8
|
1.0
|
|
C4N
|
B:NAP401
|
4.5
|
18.1
|
1.0
|
|
H1D
|
B:NAP401
|
4.5
|
18.1
|
1.0
|
|
C7N
|
B:NAP401
|
4.5
|
18.7
|
1.0
|
|
N2
|
B:CEL402
|
4.5
|
60.5
|
1.0
|
|
C3
|
B:CEL402
|
4.5
|
57.2
|
1.0
|
|
N
|
B:SER68
|
4.6
|
19.1
|
1.0
|
|
HH
|
B:TYR266
|
4.7
|
9.5
|
0.0
|
|
HA
|
B:SER68
|
4.7
|
21.0
|
1.0
|
|
C5N
|
B:NAP401
|
4.8
|
18.3
|
1.0
|
|
HB3
|
B:ALA67
|
4.8
|
19.2
|
1.0
|
|
H71N
|
B:NAP401
|
4.8
|
18.3
|
1.0
|
|
N7N
|
B:NAP401
|
4.8
|
18.1
|
1.0
|
|
CZ
|
B:TYR266
|
4.9
|
19.5
|
1.0
|
|
CE2
|
B:TYR266
|
4.9
|
19.0
|
1.0
|
|
H6N
|
B:NAP401
|
5.0
|
17.8
|
1.0
|
|
H4N
|
B:NAP401
|
5.0
|
18.1
|
1.0
|
|
Fluorine binding site 5 out
of 6 in 7zej
Go back to
Fluorine Binding Sites List in 7zej
Fluorine binding site 5 out
of 6 in the Crystal Structure of the Human MGC45594 Gene Product in Complex with Celecoxib.
 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 the Human MGC45594 Gene Product in Complex with Celecoxib. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F402
b:58.1
occ:1.00
|
F2
|
B:CEL402
|
0.0
|
58.1
|
1.0
|
|
C4
|
B:CEL402
|
1.3
|
56.4
|
1.0
|
|
F3
|
B:CEL402
|
2.1
|
40.1
|
1.0
|
|
F1
|
B:CEL402
|
2.2
|
64.3
|
1.0
|
|
C1
|
B:CEL402
|
2.3
|
57.2
|
1.0
|
|
N1
|
B:CEL402
|
2.6
|
61.0
|
1.0
|
|
HD1
|
B:PHE295
|
3.3
|
25.5
|
1.0
|
|
HE1
|
B:PHE295
|
3.4
|
26.4
|
1.0
|
|
C7N
|
B:NAP401
|
3.4
|
18.7
|
1.0
|
|
H2N
|
B:NAP401
|
3.6
|
17.2
|
1.0
|
|
C3N
|
B:NAP401
|
3.6
|
17.8
|
1.0
|
|
C2
|
B:CEL402
|
3.6
|
57.6
|
1.0
|
|
HG
|
B:SER68
|
3.6
|
12.1
|
0.0
|
|
N7N
|
B:NAP401
|
3.7
|
18.1
|
1.0
|
|
O7N
|
B:NAP401
|
3.7
|
18.9
|
1.0
|
|
C2N
|
B:NAP401
|
3.8
|
16.7
|
1.0
|
|
N2
|
B:CEL402
|
3.9
|
60.5
|
1.0
|
|
HO2N
|
B:NAP401
|
3.9
|
16.4
|
0.0
|
|
H72N
|
B:NAP401
|
3.9
|
18.3
|
1.0
|
|
CD1
|
B:PHE295
|
3.9
|
25.6
|
1.0
|
|
CE1
|
B:PHE295
|
4.0
|
26.9
|
1.0
|
|
H71N
|
B:NAP401
|
4.0
|
18.3
|
1.0
|
|
OH
|
B:TYR77
|
4.0
|
40.1
|
1.0
|
|
HC2
|
B:CEL402
|
4.1
|
57.5
|
1.0
|
|
HH
|
B:TYR77
|
4.1
|
21.9
|
0.0
|
|
HB2
|
B:SER68
|
4.3
|
23.3
|
1.0
|
|
OG
|
B:SER68
|
4.3
|
27.3
|
1.0
|
|
C4N
|
B:NAP401
|
4.4
|
18.1
|
1.0
|
|
C3
|
B:CEL402
|
4.4
|
57.2
|
1.0
|
|
H4N
|
B:NAP401
|
4.6
|
18.1
|
1.0
|
|
H17C
|
B:CEL402
|
4.6
|
58.5
|
1.0
|
|
O2D
|
B:NAP401
|
4.6
|
18.1
|
1.0
|
|
CB
|
B:SER68
|
4.7
|
22.6
|
1.0
|
|
HA
|
B:PHE295
|
4.7
|
22.6
|
1.0
|
|
C17
|
B:CEL402
|
4.7
|
59.0
|
1.0
|
|
C12
|
B:CEL402
|
4.7
|
57.4
|
1.0
|
|
N1N
|
B:NAP401
|
4.8
|
17.2
|
1.0
|
|
HB3
|
B:SER68
|
4.8
|
23.3
|
1.0
|
|
O
|
B:HOH571
|
4.8
|
14.9
|
1.0
|
|
H
|
B:LEU296
|
5.0
|
20.8
|
1.0
|
|
O
|
B:ILE260
|
5.0
|
21.1
|
1.0
|
|
Fluorine binding site 6 out
of 6 in 7zej
Go back to
Fluorine Binding Sites List in 7zej
Fluorine binding site 6 out
of 6 in the Crystal Structure of the Human MGC45594 Gene Product in Complex with Celecoxib.
 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 the Human MGC45594 Gene Product in Complex with Celecoxib. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F402
b:64.3
occ:1.00
|
F1
|
B:CEL402
|
0.0
|
64.3
|
1.0
|
|
C4
|
B:CEL402
|
1.3
|
56.4
|
1.0
|
|
F3
|
B:CEL402
|
2.2
|
40.1
|
1.0
|
|
F2
|
B:CEL402
|
2.2
|
58.1
|
1.0
|
|
C1
|
B:CEL402
|
2.3
|
57.2
|
1.0
|
|
H2N
|
B:NAP401
|
2.4
|
17.2
|
1.0
|
|
HO2N
|
B:NAP401
|
2.7
|
16.4
|
0.0
|
|
HC2
|
B:CEL402
|
2.8
|
57.5
|
1.0
|
|
C2
|
B:CEL402
|
3.0
|
57.6
|
1.0
|
|
C2N
|
B:NAP401
|
3.0
|
16.7
|
1.0
|
|
H71N
|
B:NAP401
|
3.2
|
18.3
|
1.0
|
|
O2D
|
B:NAP401
|
3.2
|
18.1
|
1.0
|
|
O
|
B:ILE260
|
3.3
|
21.1
|
1.0
|
|
N1
|
B:CEL402
|
3.3
|
61.0
|
1.0
|
|
N7N
|
B:NAP401
|
3.4
|
18.1
|
1.0
|
|
C3N
|
B:NAP401
|
3.6
|
17.8
|
1.0
|
|
OH
|
B:TYR266
|
3.6
|
19.3
|
1.0
|
|
C7N
|
B:NAP401
|
3.7
|
18.7
|
1.0
|
|
HA2
|
B:GLY261
|
3.7
|
20.0
|
1.0
|
|
HH
|
B:TYR266
|
3.7
|
9.5
|
0.0
|
|
H72N
|
B:NAP401
|
3.7
|
18.3
|
1.0
|
|
H1D
|
B:NAP401
|
3.8
|
18.1
|
1.0
|
|
HG
|
B:SER68
|
3.9
|
12.1
|
0.0
|
|
N1N
|
B:NAP401
|
3.9
|
17.2
|
1.0
|
|
HA3
|
B:GLY261
|
4.0
|
20.0
|
1.0
|
|
C3
|
B:CEL402
|
4.1
|
57.2
|
1.0
|
|
C1D
|
B:NAP401
|
4.2
|
18.2
|
1.0
|
|
C2D
|
B:NAP401
|
4.2
|
18.4
|
1.0
|
|
N2
|
B:CEL402
|
4.2
|
60.5
|
1.0
|
|
CA
|
B:GLY261
|
4.3
|
19.7
|
1.0
|
|
C
|
B:ILE260
|
4.4
|
19.6
|
1.0
|
|
OG
|
B:SER68
|
4.4
|
27.3
|
1.0
|
|
O7N
|
B:NAP401
|
4.5
|
18.9
|
1.0
|
|
HD1
|
B:PHE295
|
4.7
|
25.5
|
1.0
|
|
C4N
|
B:NAP401
|
4.7
|
18.1
|
1.0
|
|
H2D
|
B:NAP401
|
4.7
|
18.4
|
1.0
|
|
HB2
|
B:SER68
|
4.7
|
23.3
|
1.0
|
|
CZ
|
B:TYR266
|
4.8
|
19.5
|
1.0
|
|
N
|
B:GLY261
|
4.8
|
20.4
|
1.0
|
|
HO3N
|
B:NAP401
|
4.9
|
25.8
|
0.0
|
|
O
|
B:HOH571
|
4.9
|
14.9
|
1.0
|
|
C6N
|
B:NAP401
|
4.9
|
17.8
|
1.0
|
|
Reference:
N.Shafqat,
S.G.Dakin,
F.M.Estrada,
F.H.Niesen,
G.Wells,
C.Yapp,
M.K.Troumpra,
D.Brotherton,
S.Porte,
J.Mesa,
E.Yakovtseva,
J.Farres,
X.Pares,
T.Liu,
R.Altman,
A.Carr,
L.Koekemoer,
F.Niesen,
W.W.Yue,
U.Opperman.
Human Prostaglandin/Alkenal Reductases: Substrate Specificities, Inhibitor Profiles, Structural Insights and Subcellular Localization Suggest Protective Roles in Inflammatory and Oxidative Stress Conditions. To Be Published.
Page generated: Wed Apr 5 02:00:10 2023
|
