Fluorine in PDB 5lws: Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof
Enzymatic activity of Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof
All present enzymatic activity of Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof:
3.4.23.22;
Protein crystallography data
The structure of Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof, PDB code: 5lws
was solved by
J.Schiebel,
A.Heine,
G.Klebe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
36.55 /
1.03
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
45.327,
73.095,
53.029,
90.00,
109.83,
90.00
|
|
R / Rfree (%)
|
11.6 /
13.2
|
Other elements in 5lws:
The structure of Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof
(pdb code 5lws). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the
Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof, PDB code: 5lws:
Jump to Fluorine binding site number:
1;
2;
3;
4;
5;
6;
Fluorine binding site 1 out
of 6 in 5lws
Go back to
Fluorine Binding Sites List in 5lws
Fluorine binding site 1 out
of 6 in the Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F411
b:23.8
occ:0.57
|
F1
|
A:TFA411
|
0.0
|
23.8
|
0.6
|
|
C1
|
A:TFA411
|
0.3
|
35.6
|
0.4
|
|
O
|
A:TFA411
|
1.3
|
35.6
|
0.4
|
|
C2
|
A:TFA411
|
1.4
|
20.9
|
0.6
|
|
OXT
|
A:TFA411
|
1.4
|
36.0
|
0.4
|
|
C2
|
A:TFA411
|
1.4
|
34.1
|
0.4
|
|
F3
|
A:TFA411
|
2.2
|
30.4
|
0.4
|
|
F2
|
A:TFA411
|
2.2
|
35.6
|
0.4
|
|
F3
|
A:TFA411
|
2.2
|
18.4
|
0.6
|
|
F2
|
A:TFA411
|
2.3
|
21.1
|
0.6
|
|
C1
|
A:TFA411
|
2.4
|
22.3
|
0.6
|
|
F1
|
A:TFA411
|
2.4
|
34.6
|
0.4
|
|
HG
|
A:SER289
|
3.1
|
9.9
|
0.3
|
|
O
|
A:TFA411
|
3.1
|
26.0
|
0.6
|
|
OXT
|
A:TFA411
|
3.1
|
18.2
|
0.6
|
|
HG23
|
A:VAL252
|
3.2
|
13.3
|
1.0
|
|
CE
|
A:LYS243
|
3.4
|
22.2
|
1.0
|
|
HG21
|
A:VAL252
|
3.6
|
13.3
|
1.0
|
|
OG
|
A:SER289
|
3.6
|
12.2
|
0.7
|
|
OG
|
A:SER289
|
3.6
|
8.2
|
0.3
|
|
O
|
A:HOH2468
|
3.7
|
31.5
|
1.0
|
|
HG2
|
A:LYS243
|
3.8
|
18.2
|
1.0
|
|
HB3
|
A:SER289
|
3.9
|
10.9
|
0.7
|
|
CG2
|
A:VAL252
|
3.9
|
11.1
|
1.0
|
|
HB2
|
A:SER289
|
3.9
|
9.2
|
0.3
|
|
O
|
A:HOH2492
|
3.9
|
46.1
|
1.0
|
|
HD3
|
A:LYS243
|
4.1
|
23.4
|
1.0
|
|
CD
|
A:LYS243
|
4.2
|
19.5
|
1.0
|
|
HG
|
A:SER289
|
4.3
|
14.7
|
0.7
|
|
CB
|
A:SER289
|
4.3
|
9.1
|
0.7
|
|
CB
|
A:SER289
|
4.3
|
7.7
|
0.3
|
|
CG
|
A:LYS243
|
4.5
|
15.2
|
1.0
|
|
O
|
A:GLY241
|
4.5
|
12.0
|
1.0
|
|
HB
|
A:VAL252
|
4.6
|
10.5
|
1.0
|
|
HG22
|
A:VAL252
|
4.6
|
13.3
|
1.0
|
|
HA
|
A:SER289
|
4.7
|
9.2
|
0.3
|
|
HA
|
A:SER289
|
4.7
|
9.6
|
0.7
|
|
HA
|
A:PHE253
|
4.8
|
8.3
|
1.0
|
|
HG3
|
A:LYS243
|
4.8
|
18.2
|
1.0
|
|
CB
|
A:VAL252
|
4.9
|
8.8
|
1.0
|
|
HD3
|
A:PRO254
|
4.9
|
11.2
|
1.0
|
|
HG3
|
A:PRO254
|
5.0
|
12.5
|
1.0
|
|
Fluorine binding site 2 out
of 6 in 5lws
Go back to
Fluorine Binding Sites List in 5lws
Fluorine binding site 2 out
of 6 in the Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F411
b:34.6
occ:0.43
|
F1
|
A:TFA411
|
0.0
|
34.6
|
0.4
|
|
C1
|
A:TFA411
|
0.1
|
22.3
|
0.6
|
|
OXT
|
A:TFA411
|
1.2
|
18.2
|
0.6
|
|
O
|
A:TFA411
|
1.3
|
26.0
|
0.6
|
|
C2
|
A:TFA411
|
1.4
|
34.1
|
0.4
|
|
C2
|
A:TFA411
|
1.6
|
20.9
|
0.6
|
|
F3
|
A:TFA411
|
2.2
|
30.4
|
0.4
|
|
F2
|
A:TFA411
|
2.2
|
35.6
|
0.4
|
|
F3
|
A:TFA411
|
2.4
|
18.4
|
0.6
|
|
C1
|
A:TFA411
|
2.4
|
35.6
|
0.4
|
|
F2
|
A:TFA411
|
2.4
|
21.1
|
0.6
|
|
F1
|
A:TFA411
|
2.4
|
23.8
|
0.6
|
|
OXT
|
A:TFA411
|
3.0
|
36.0
|
0.4
|
|
HA
|
A:PRO254
|
3.1
|
10.3
|
1.0
|
|
HG3
|
A:PRO254
|
3.1
|
12.5
|
1.0
|
|
O
|
A:TFA411
|
3.2
|
35.6
|
0.4
|
|
O
|
A:HOH2483
|
3.5
|
12.8
|
1.0
|
|
HG
|
A:SER289
|
3.6
|
9.9
|
0.3
|
|
OG
|
A:SER289
|
3.6
|
12.2
|
0.7
|
|
CA
|
A:PRO254
|
3.7
|
8.6
|
1.0
|
|
HA
|
A:SER289
|
3.7
|
9.6
|
0.7
|
|
HA
|
A:SER289
|
3.7
|
9.2
|
0.3
|
|
N
|
A:PRO254
|
3.7
|
8.1
|
1.0
|
|
CG
|
A:PRO254
|
3.8
|
10.4
|
1.0
|
|
O
|
A:HOH2468
|
3.8
|
31.5
|
1.0
|
|
HB3
|
A:PRO254
|
3.9
|
12.7
|
1.0
|
|
HD3
|
A:PRO254
|
3.9
|
11.2
|
1.0
|
|
HB2
|
A:SER289
|
3.9
|
9.2
|
0.3
|
|
HG
|
A:SER289
|
4.0
|
14.7
|
0.7
|
|
CB
|
A:PRO254
|
4.0
|
10.5
|
1.0
|
|
CD
|
A:PRO254
|
4.1
|
9.3
|
1.0
|
|
C
|
A:PHE253
|
4.1
|
6.8
|
1.0
|
|
OG
|
A:SER289
|
4.3
|
8.2
|
0.3
|
|
HB3
|
A:SER289
|
4.3
|
10.9
|
0.7
|
|
O
|
A:PHE253
|
4.3
|
7.0
|
1.0
|
|
CB
|
A:SER289
|
4.3
|
9.1
|
0.7
|
|
CB
|
A:SER289
|
4.4
|
7.7
|
0.3
|
|
CA
|
A:SER289
|
4.4
|
8.0
|
0.7
|
|
CA
|
A:SER289
|
4.4
|
7.7
|
0.3
|
|
HA
|
A:PHE253
|
4.5
|
8.3
|
1.0
|
|
O
|
A:SER288
|
4.6
|
9.1
|
1.0
|
|
HG2
|
A:PRO254
|
4.6
|
12.5
|
1.0
|
|
O
|
A:GLY241
|
4.6
|
12.0
|
1.0
|
|
CA
|
A:PHE253
|
4.8
|
7.0
|
1.0
|
|
HG23
|
A:VAL252
|
4.9
|
13.3
|
1.0
|
|
O
|
A:HOH2492
|
4.9
|
46.1
|
1.0
|
|
Fluorine binding site 3 out
of 6 in 5lws
Go back to
Fluorine Binding Sites List in 5lws
Fluorine binding site 3 out
of 6 in the Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F411
b:21.1
occ:0.57
|
F2
|
A:TFA411
|
0.0
|
21.1
|
0.6
|
|
F2
|
A:TFA411
|
0.2
|
35.6
|
0.4
|
|
C2
|
A:TFA411
|
1.4
|
20.9
|
0.6
|
|
C2
|
A:TFA411
|
1.5
|
34.1
|
0.4
|
|
F3
|
A:TFA411
|
2.1
|
18.4
|
0.6
|
|
F3
|
A:TFA411
|
2.2
|
30.4
|
0.4
|
|
F1
|
A:TFA411
|
2.3
|
23.8
|
0.6
|
|
C1
|
A:TFA411
|
2.4
|
22.3
|
0.6
|
|
F1
|
A:TFA411
|
2.4
|
34.6
|
0.4
|
|
C1
|
A:TFA411
|
2.5
|
35.6
|
0.4
|
|
HA
|
A:PHE253
|
2.7
|
8.3
|
1.0
|
|
HD3
|
A:PRO254
|
2.8
|
11.2
|
1.0
|
|
O
|
A:TFA411
|
2.8
|
26.0
|
0.6
|
|
O
|
A:GLY241
|
2.8
|
12.0
|
1.0
|
|
OXT
|
A:TFA411
|
2.9
|
36.0
|
0.4
|
|
HG23
|
A:VAL252
|
3.2
|
13.3
|
1.0
|
|
O
|
A:HOH2468
|
3.3
|
31.5
|
1.0
|
|
CA
|
A:PHE253
|
3.4
|
7.0
|
1.0
|
|
OXT
|
A:TFA411
|
3.4
|
18.2
|
0.6
|
|
HG3
|
A:PRO254
|
3.4
|
12.5
|
1.0
|
|
O
|
A:TFA411
|
3.5
|
35.6
|
0.4
|
|
CD
|
A:PRO254
|
3.5
|
9.3
|
1.0
|
|
C
|
A:PHE253
|
3.5
|
6.8
|
1.0
|
|
HA
|
A:ALA242
|
3.5
|
10.6
|
1.0
|
|
N
|
A:PRO254
|
3.5
|
8.1
|
1.0
|
|
HG2
|
A:LYS243
|
3.6
|
18.2
|
1.0
|
|
HG
|
A:SER289
|
3.7
|
9.9
|
0.3
|
|
N
|
A:PHE253
|
3.8
|
7.0
|
1.0
|
|
C
|
A:GLY241
|
3.8
|
10.1
|
1.0
|
|
O
|
A:VAL252
|
3.8
|
8.4
|
1.0
|
|
C
|
A:VAL252
|
4.0
|
7.3
|
1.0
|
|
CG
|
A:PRO254
|
4.0
|
10.4
|
1.0
|
|
HA
|
A:PRO254
|
4.1
|
10.3
|
1.0
|
|
CG2
|
A:VAL252
|
4.1
|
11.1
|
1.0
|
|
O
|
A:PHE253
|
4.2
|
7.0
|
1.0
|
|
H
|
A:PHE253
|
4.2
|
8.4
|
1.0
|
|
CA
|
A:ALA242
|
4.3
|
8.9
|
1.0
|
|
HD2
|
A:PRO254
|
4.3
|
11.2
|
1.0
|
|
H
|
A:LYS243
|
4.3
|
11.5
|
1.0
|
|
CA
|
A:PRO254
|
4.3
|
8.6
|
1.0
|
|
HG21
|
A:VAL252
|
4.4
|
13.3
|
1.0
|
|
HA3
|
A:GLY241
|
4.5
|
13.5
|
1.0
|
|
N
|
A:ALA242
|
4.5
|
9.1
|
1.0
|
|
OG
|
A:SER289
|
4.5
|
8.2
|
0.3
|
|
HB
|
A:VAL252
|
4.5
|
10.5
|
1.0
|
|
CG
|
A:LYS243
|
4.5
|
15.2
|
1.0
|
|
HD3
|
A:LYS243
|
4.6
|
23.4
|
1.0
|
|
CE
|
A:LYS243
|
4.6
|
22.2
|
1.0
|
|
N
|
A:LYS243
|
4.7
|
9.6
|
1.0
|
|
HG2
|
A:PRO254
|
4.7
|
12.5
|
1.0
|
|
HG22
|
A:VAL252
|
4.7
|
13.3
|
1.0
|
|
CA
|
A:GLY241
|
4.7
|
11.2
|
1.0
|
|
HB3
|
A:SER289
|
4.7
|
10.9
|
0.7
|
|
O
|
A:HOH2492
|
4.8
|
46.1
|
1.0
|
|
C
|
A:ALA242
|
4.8
|
9.5
|
1.0
|
|
CB
|
A:PHE253
|
4.8
|
7.8
|
1.0
|
|
CB
|
A:PRO254
|
4.8
|
10.5
|
1.0
|
|
HA
|
A:SER289
|
4.8
|
9.6
|
0.7
|
|
CB
|
A:VAL252
|
4.8
|
8.8
|
1.0
|
|
HA
|
A:SER289
|
4.8
|
9.2
|
0.3
|
|
CD
|
A:LYS243
|
4.8
|
19.5
|
1.0
|
|
HB2
|
A:PHE253
|
4.9
|
9.4
|
1.0
|
|
OG
|
A:SER289
|
5.0
|
12.2
|
0.7
|
|
Fluorine binding site 4 out
of 6 in 5lws
Go back to
Fluorine Binding Sites List in 5lws
Fluorine binding site 4 out
of 6 in the Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 4 of Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F411
b:35.6
occ:0.43
|
F2
|
A:TFA411
|
0.0
|
35.6
|
0.4
|
|
F2
|
A:TFA411
|
0.2
|
21.1
|
0.6
|
|
C2
|
A:TFA411
|
1.3
|
20.9
|
0.6
|
|
C2
|
A:TFA411
|
1.4
|
34.1
|
0.4
|
|
C1
|
A:TFA411
|
2.2
|
22.3
|
0.6
|
|
F1
|
A:TFA411
|
2.2
|
23.8
|
0.6
|
|
F3
|
A:TFA411
|
2.2
|
18.4
|
0.6
|
|
F3
|
A:TFA411
|
2.2
|
30.4
|
0.4
|
|
F1
|
A:TFA411
|
2.2
|
34.6
|
0.4
|
|
C1
|
A:TFA411
|
2.4
|
35.6
|
0.4
|
|
O
|
A:TFA411
|
2.5
|
26.0
|
0.6
|
|
OXT
|
A:TFA411
|
2.8
|
36.0
|
0.4
|
|
HD3
|
A:PRO254
|
2.8
|
11.2
|
1.0
|
|
O
|
A:GLY241
|
2.8
|
12.0
|
1.0
|
|
HA
|
A:PHE253
|
2.9
|
8.3
|
1.0
|
|
O
|
A:HOH2468
|
3.1
|
31.5
|
1.0
|
|
OXT
|
A:TFA411
|
3.3
|
18.2
|
0.6
|
|
HG3
|
A:PRO254
|
3.3
|
12.5
|
1.0
|
|
HG23
|
A:VAL252
|
3.4
|
13.3
|
1.0
|
|
O
|
A:TFA411
|
3.4
|
35.6
|
0.4
|
|
CD
|
A:PRO254
|
3.5
|
9.3
|
1.0
|
|
N
|
A:PRO254
|
3.5
|
8.1
|
1.0
|
|
C
|
A:PHE253
|
3.6
|
6.8
|
1.0
|
|
CA
|
A:PHE253
|
3.6
|
7.0
|
1.0
|
|
HA
|
A:ALA242
|
3.7
|
10.6
|
1.0
|
|
HG2
|
A:LYS243
|
3.7
|
18.2
|
1.0
|
|
HG
|
A:SER289
|
3.8
|
9.9
|
0.3
|
|
C
|
A:GLY241
|
3.8
|
10.1
|
1.0
|
|
CG
|
A:PRO254
|
3.9
|
10.4
|
1.0
|
|
N
|
A:PHE253
|
4.0
|
7.0
|
1.0
|
|
O
|
A:VAL252
|
4.1
|
8.4
|
1.0
|
|
HA
|
A:PRO254
|
4.1
|
10.3
|
1.0
|
|
C
|
A:VAL252
|
4.2
|
7.3
|
1.0
|
|
O
|
A:PHE253
|
4.3
|
7.0
|
1.0
|
|
CA
|
A:PRO254
|
4.3
|
8.6
|
1.0
|
|
CG2
|
A:VAL252
|
4.3
|
11.1
|
1.0
|
|
HD2
|
A:PRO254
|
4.3
|
11.2
|
1.0
|
|
HA3
|
A:GLY241
|
4.3
|
13.5
|
1.0
|
|
H
|
A:PHE253
|
4.4
|
8.4
|
1.0
|
|
CA
|
A:ALA242
|
4.4
|
8.9
|
1.0
|
|
H
|
A:LYS243
|
4.5
|
11.5
|
1.0
|
|
N
|
A:ALA242
|
4.5
|
9.1
|
1.0
|
|
HG21
|
A:VAL252
|
4.5
|
13.3
|
1.0
|
|
HD3
|
A:LYS243
|
4.6
|
23.4
|
1.0
|
|
OG
|
A:SER289
|
4.6
|
8.2
|
0.3
|
|
HG2
|
A:PRO254
|
4.6
|
12.5
|
1.0
|
|
O
|
A:HOH2492
|
4.6
|
46.1
|
1.0
|
|
CG
|
A:LYS243
|
4.6
|
15.2
|
1.0
|
|
CE
|
A:LYS243
|
4.6
|
22.2
|
1.0
|
|
CA
|
A:GLY241
|
4.7
|
11.2
|
1.0
|
|
CB
|
A:PRO254
|
4.7
|
10.5
|
1.0
|
|
HB
|
A:VAL252
|
4.7
|
10.5
|
1.0
|
|
HB3
|
A:SER289
|
4.8
|
10.9
|
0.7
|
|
HA
|
A:SER289
|
4.8
|
9.6
|
0.7
|
|
HA
|
A:SER289
|
4.8
|
9.2
|
0.3
|
|
N
|
A:LYS243
|
4.8
|
9.6
|
1.0
|
|
CD
|
A:LYS243
|
4.9
|
19.5
|
1.0
|
|
C
|
A:ALA242
|
4.9
|
9.5
|
1.0
|
|
HG22
|
A:VAL252
|
4.9
|
13.3
|
1.0
|
|
OG
|
A:SER289
|
4.9
|
12.2
|
0.7
|
|
HB3
|
A:PRO254
|
4.9
|
12.7
|
1.0
|
|
CB
|
A:PHE253
|
4.9
|
7.8
|
1.0
|
|
HA2
|
A:GLY241
|
4.9
|
13.5
|
1.0
|
|
Fluorine binding site 5 out
of 6 in 5lws
Go back to
Fluorine Binding Sites List in 5lws
Fluorine binding site 5 out
of 6 in the Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 5 of Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F411
b:18.4
occ:0.57
|
F3
|
A:TFA411
|
0.0
|
18.4
|
0.6
|
|
F3
|
A:TFA411
|
0.2
|
30.4
|
0.4
|
|
C2
|
A:TFA411
|
1.3
|
20.9
|
0.6
|
|
C2
|
A:TFA411
|
1.4
|
34.1
|
0.4
|
|
HG
|
A:SER289
|
1.6
|
9.9
|
0.3
|
|
F2
|
A:TFA411
|
2.1
|
21.1
|
0.6
|
|
F2
|
A:TFA411
|
2.2
|
35.6
|
0.4
|
|
F1
|
A:TFA411
|
2.2
|
23.8
|
0.6
|
|
C1
|
A:TFA411
|
2.3
|
22.3
|
0.6
|
|
F1
|
A:TFA411
|
2.4
|
34.6
|
0.4
|
|
C1
|
A:TFA411
|
2.4
|
35.6
|
0.4
|
|
OG
|
A:SER289
|
2.4
|
8.2
|
0.3
|
|
OXT
|
A:TFA411
|
2.6
|
18.2
|
0.6
|
|
HB3
|
A:SER289
|
2.6
|
10.9
|
0.7
|
|
O
|
A:TFA411
|
2.6
|
35.6
|
0.4
|
|
HA
|
A:SER289
|
2.9
|
9.2
|
0.3
|
|
HA
|
A:SER289
|
2.9
|
9.6
|
0.7
|
|
HG23
|
A:VAL252
|
3.0
|
13.3
|
1.0
|
|
OG
|
A:SER289
|
3.2
|
12.2
|
0.7
|
|
CB
|
A:SER289
|
3.2
|
9.1
|
0.7
|
|
HB2
|
A:SER289
|
3.2
|
9.2
|
0.3
|
|
CB
|
A:SER289
|
3.2
|
7.7
|
0.3
|
|
HB
|
A:VAL252
|
3.2
|
10.5
|
1.0
|
|
O
|
A:PHE253
|
3.2
|
7.0
|
1.0
|
|
C
|
A:PHE253
|
3.2
|
6.8
|
1.0
|
|
H
|
A:PHE253
|
3.4
|
8.4
|
1.0
|
|
N
|
A:PHE253
|
3.4
|
7.0
|
1.0
|
|
O
|
A:TFA411
|
3.5
|
26.0
|
0.6
|
|
HA
|
A:PHE253
|
3.5
|
8.3
|
1.0
|
|
CA
|
A:SER289
|
3.5
|
8.0
|
0.7
|
|
CA
|
A:SER289
|
3.5
|
7.7
|
0.3
|
|
OXT
|
A:TFA411
|
3.5
|
36.0
|
0.4
|
|
CG2
|
A:VAL252
|
3.6
|
11.1
|
1.0
|
|
HG21
|
A:VAL252
|
3.6
|
13.3
|
1.0
|
|
CA
|
A:PHE253
|
3.6
|
7.0
|
1.0
|
|
H
|
A:CYS290
|
3.6
|
8.6
|
1.0
|
|
HA
|
A:PRO254
|
3.7
|
10.3
|
1.0
|
|
N
|
A:PRO254
|
3.7
|
8.1
|
1.0
|
|
CB
|
A:VAL252
|
3.8
|
8.8
|
1.0
|
|
HG
|
A:SER289
|
3.9
|
14.7
|
0.7
|
|
C
|
A:VAL252
|
3.9
|
7.3
|
1.0
|
|
HB2
|
A:SER289
|
4.1
|
10.9
|
0.7
|
|
HB3
|
A:SER289
|
4.1
|
9.2
|
0.3
|
|
HD3
|
A:PRO254
|
4.1
|
11.2
|
1.0
|
|
N
|
A:CYS290
|
4.2
|
7.1
|
1.0
|
|
CA
|
A:PRO254
|
4.2
|
8.6
|
1.0
|
|
C
|
A:SER289
|
4.3
|
7.3
|
0.3
|
|
C
|
A:SER289
|
4.3
|
7.3
|
0.7
|
|
O
|
A:VAL252
|
4.4
|
8.4
|
1.0
|
|
CD
|
A:PRO254
|
4.5
|
9.3
|
1.0
|
|
HG22
|
A:VAL252
|
4.5
|
13.3
|
1.0
|
|
CA
|
A:VAL252
|
4.5
|
7.6
|
1.0
|
|
HG3
|
A:PRO254
|
4.5
|
12.5
|
1.0
|
|
N
|
A:SER289
|
4.7
|
7.2
|
0.7
|
|
N
|
A:SER289
|
4.7
|
7.6
|
0.3
|
|
O
|
A:CYS290
|
4.8
|
8.2
|
1.0
|
|
HG2
|
A:LYS243
|
4.8
|
18.2
|
1.0
|
|
O
|
A:SER288
|
4.9
|
9.1
|
1.0
|
|
CG
|
A:PRO254
|
4.9
|
10.4
|
1.0
|
|
HA
|
A:VAL252
|
5.0
|
9.1
|
1.0
|
|
O
|
A:GLY241
|
5.0
|
12.0
|
1.0
|
|
Fluorine binding site 6 out
of 6 in 5lws
Go back to
Fluorine Binding Sites List in 5lws
Fluorine binding site 6 out
of 6 in the Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 6 of Endothiapepsin in Complex with Fragment 177 and A Derivative Thereof within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F411
b:30.4
occ:0.43
|
F3
|
A:TFA411
|
0.0
|
30.4
|
0.4
|
|
F3
|
A:TFA411
|
0.2
|
18.4
|
0.6
|
|
C2
|
A:TFA411
|
1.3
|
20.9
|
0.6
|
|
C2
|
A:TFA411
|
1.4
|
34.1
|
0.4
|
|
HG
|
A:SER289
|
1.6
|
9.9
|
0.3
|
|
F2
|
A:TFA411
|
2.2
|
21.1
|
0.6
|
|
F1
|
A:TFA411
|
2.2
|
23.8
|
0.6
|
|
C1
|
A:TFA411
|
2.2
|
22.3
|
0.6
|
|
F2
|
A:TFA411
|
2.2
|
35.6
|
0.4
|
|
F1
|
A:TFA411
|
2.2
|
34.6
|
0.4
|
|
C1
|
A:TFA411
|
2.3
|
35.6
|
0.4
|
|
OXT
|
A:TFA411
|
2.5
|
18.2
|
0.6
|
|
OG
|
A:SER289
|
2.5
|
8.2
|
0.3
|
|
O
|
A:TFA411
|
2.6
|
35.6
|
0.4
|
|
HB3
|
A:SER289
|
2.6
|
10.9
|
0.7
|
|
HA
|
A:SER289
|
2.8
|
9.2
|
0.3
|
|
HA
|
A:SER289
|
2.8
|
9.6
|
0.7
|
|
OG
|
A:SER289
|
3.1
|
12.2
|
0.7
|
|
HB2
|
A:SER289
|
3.1
|
9.2
|
0.3
|
|
HG23
|
A:VAL252
|
3.1
|
13.3
|
1.0
|
|
CB
|
A:SER289
|
3.1
|
9.1
|
0.7
|
|
CB
|
A:SER289
|
3.2
|
7.7
|
0.3
|
|
O
|
A:PHE253
|
3.2
|
7.0
|
1.0
|
|
C
|
A:PHE253
|
3.3
|
6.8
|
1.0
|
|
O
|
A:TFA411
|
3.4
|
26.0
|
0.6
|
|
HB
|
A:VAL252
|
3.4
|
10.5
|
1.0
|
|
CA
|
A:SER289
|
3.4
|
8.0
|
0.7
|
|
CA
|
A:SER289
|
3.4
|
7.7
|
0.3
|
|
OXT
|
A:TFA411
|
3.5
|
36.0
|
0.4
|
|
H
|
A:PHE253
|
3.5
|
8.4
|
1.0
|
|
N
|
A:PHE253
|
3.5
|
7.0
|
1.0
|
|
HA
|
A:PRO254
|
3.6
|
10.3
|
1.0
|
|
HA
|
A:PHE253
|
3.6
|
8.3
|
1.0
|
|
H
|
A:CYS290
|
3.6
|
8.6
|
1.0
|
|
CA
|
A:PHE253
|
3.7
|
7.0
|
1.0
|
|
N
|
A:PRO254
|
3.7
|
8.1
|
1.0
|
|
HG21
|
A:VAL252
|
3.7
|
13.3
|
1.0
|
|
CG2
|
A:VAL252
|
3.7
|
11.1
|
1.0
|
|
HG
|
A:SER289
|
3.8
|
14.7
|
0.7
|
|
CB
|
A:VAL252
|
4.0
|
8.8
|
1.0
|
|
HB2
|
A:SER289
|
4.0
|
10.9
|
0.7
|
|
C
|
A:VAL252
|
4.1
|
7.3
|
1.0
|
|
HB3
|
A:SER289
|
4.1
|
9.2
|
0.3
|
|
HD3
|
A:PRO254
|
4.1
|
11.2
|
1.0
|
|
CA
|
A:PRO254
|
4.1
|
8.6
|
1.0
|
|
N
|
A:CYS290
|
4.2
|
7.1
|
1.0
|
|
C
|
A:SER289
|
4.3
|
7.3
|
0.3
|
|
C
|
A:SER289
|
4.3
|
7.3
|
0.7
|
|
CD
|
A:PRO254
|
4.4
|
9.3
|
1.0
|
|
HG3
|
A:PRO254
|
4.4
|
12.5
|
1.0
|
|
O
|
A:VAL252
|
4.5
|
8.4
|
1.0
|
|
N
|
A:SER289
|
4.6
|
7.2
|
0.7
|
|
N
|
A:SER289
|
4.6
|
7.6
|
0.3
|
|
HG22
|
A:VAL252
|
4.6
|
13.3
|
1.0
|
|
CA
|
A:VAL252
|
4.7
|
7.6
|
1.0
|
|
O
|
A:SER288
|
4.8
|
9.1
|
1.0
|
|
O
|
A:CYS290
|
4.9
|
8.2
|
1.0
|
|
HG2
|
A:LYS243
|
4.9
|
18.2
|
1.0
|
|
CG
|
A:PRO254
|
4.9
|
10.4
|
1.0
|
|
Reference:
J.Cramer,
J.Schiebel,
T.Wulsdorf,
K.Grohe,
E.E.Najbauer,
F.R.Ehrmann,
N.Radeva,
N.Zitzer,
U.Linne,
R.Linser,
A.Heine,
G.Klebe.
A False-Positive Screening Hit in Fragment-Based Lead Discovery: Watch Out For the Red Herring. Angew. Chem. Int. Ed. Engl. V. 56 1908 2017.
ISSN: ESSN 1521-3773
PubMed: 28097765
DOI: 10.1002/ANIE.201609824
Page generated: Thu Aug 1 11:31:14 2024
|
