Fluorine in PDB 5rcf: Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B
Enzymatic activity of Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B
All present enzymatic activity of Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B:
3.4.23.22;
Protein crystallography data
The structure of Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B, PDB code: 5rcf
was solved by
M.S.Weiss,
J.Wollenhaupt,
A.Metz,
T.Barthel,
G.M.A.Lima,
A.Heine,
U.Mueller,
G.Klebe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
42.76 /
1.00
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
45.190,
73.182,
52.406,
90.00,
109.01,
90.00
|
|
R / Rfree (%)
|
15.5 /
15.6
|
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B
(pdb code 5rcf). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the
Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B, PDB code: 5rcf:
Jump to Fluorine binding site number:
1;
2;
3;
4;
Fluorine binding site 1 out
of 4 in 5rcf
Go back to
Fluorine Binding Sites List in 5rcf
Fluorine binding site 1 out
of 4 in the Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F401
b:11.4
occ:0.28
|
F
|
A:RE7401
|
0.0
|
11.4
|
0.3
|
|
F
|
A:RE7401
|
0.0
|
11.7
|
0.1
|
|
C5
|
A:RE7401
|
1.4
|
11.4
|
0.3
|
|
C5
|
A:RE7401
|
1.4
|
11.6
|
0.1
|
|
O4
|
A:PG4411
|
1.9
|
49.5
|
0.3
|
|
C7
|
A:PG4411
|
1.9
|
51.7
|
0.3
|
|
O4
|
A:PG4411
|
2.0
|
50.5
|
0.3
|
|
C7
|
A:PG4411
|
2.0
|
52.8
|
0.3
|
|
C6
|
A:RE7401
|
2.3
|
11.8
|
0.1
|
|
C6
|
A:RE7401
|
2.3
|
11.9
|
0.3
|
|
C4
|
A:RE7401
|
2.3
|
10.9
|
0.3
|
|
C4
|
A:RE7401
|
2.4
|
11.3
|
0.1
|
|
C6
|
A:PG4411
|
2.5
|
48.5
|
0.3
|
|
C6
|
A:PG4411
|
2.6
|
49.5
|
0.3
|
|
C8
|
A:PG4411
|
3.1
|
52.0
|
0.3
|
|
CA
|
A:ILE283
|
3.1
|
10.5
|
0.3
|
|
CA
|
A:ILE283
|
3.1
|
10.5
|
0.3
|
|
C8
|
A:PG4411
|
3.2
|
53.0
|
0.3
|
|
O
|
A:ILE283
|
3.3
|
12.6
|
0.3
|
|
O
|
A:ILE283
|
3.3
|
12.6
|
0.3
|
|
CG2
|
A:ILE283
|
3.3
|
9.8
|
0.1
|
|
CA
|
A:ILE283
|
3.3
|
8.5
|
0.1
|
|
CG2
|
A:ILE283
|
3.3
|
11.8
|
0.3
|
|
CB
|
A:ILE283
|
3.4
|
9.3
|
0.1
|
|
CA
|
A:ILE283
|
3.4
|
9.4
|
0.3
|
|
CD1
|
A:PHE291
|
3.4
|
10.9
|
0.3
|
|
O5
|
A:PG4411
|
3.4
|
52.5
|
0.3
|
|
CB
|
A:ILE283
|
3.4
|
10.8
|
0.3
|
|
CD1
|
A:PHE291
|
3.4
|
10.4
|
0.1
|
|
O
|
A:HOH689
|
3.4
|
20.9
|
0.3
|
|
C5
|
A:PG4411
|
3.4
|
48.0
|
0.3
|
|
O5
|
A:PG4411
|
3.4
|
51.4
|
0.3
|
|
C5
|
A:PG4411
|
3.5
|
48.8
|
0.3
|
|
CB
|
A:ILE283
|
3.5
|
11.6
|
0.3
|
|
CB
|
A:ILE283
|
3.5
|
11.6
|
0.3
|
|
CG
|
A:PHE291
|
3.5
|
9.8
|
0.3
|
|
CG
|
A:PHE291
|
3.5
|
9.9
|
0.1
|
|
CB
|
A:PHE291
|
3.6
|
9.6
|
0.1
|
|
C7
|
A:RE7401
|
3.6
|
11.7
|
0.1
|
|
C7
|
A:RE7401
|
3.6
|
11.5
|
0.3
|
|
CB
|
A:PHE291
|
3.6
|
9.4
|
0.3
|
|
C3
|
A:RE7401
|
3.6
|
11.6
|
0.3
|
|
C3
|
A:RE7401
|
3.6
|
11.7
|
0.1
|
|
CB
|
A:PHE291
|
3.6
|
9.8
|
0.3
|
|
CB
|
A:PHE291
|
3.6
|
9.8
|
0.3
|
|
C
|
A:ILE283
|
3.7
|
10.5
|
0.3
|
|
C
|
A:ILE283
|
3.7
|
10.5
|
0.3
|
|
CG2
|
A:ILE283
|
3.7
|
12.2
|
0.3
|
|
CG2
|
A:ILE283
|
3.7
|
12.2
|
0.3
|
|
O
|
A:HOH565
|
3.7
|
21.4
|
0.3
|
|
CG
|
A:PHE291
|
3.8
|
9.7
|
0.3
|
|
CG
|
A:PHE291
|
3.8
|
9.7
|
0.3
|
|
O
|
A:ILE283
|
3.8
|
6.8
|
0.1
|
|
O
|
A:ILE283
|
3.8
|
14.2
|
0.3
|
|
CG1
|
A:VAL248
|
3.8
|
15.9
|
0.1
|
|
CD1
|
A:PHE291
|
3.9
|
10.3
|
0.3
|
|
CD1
|
A:PHE291
|
3.9
|
10.3
|
0.3
|
|
O3
|
A:PG4411
|
4.0
|
47.6
|
0.3
|
|
O3
|
A:PG4411
|
4.0
|
48.3
|
0.3
|
|
CG1
|
A:VAL248
|
4.0
|
16.8
|
0.3
|
|
C
|
A:ILE283
|
4.1
|
8.4
|
0.1
|
|
C
|
A:ILE283
|
4.1
|
10.1
|
0.3
|
|
C2
|
A:RE7401
|
4.1
|
11.6
|
0.3
|
|
C2
|
A:RE7401
|
4.1
|
11.8
|
0.1
|
|
CE1
|
A:PHE291
|
4.2
|
11.8
|
0.3
|
|
CG1
|
A:VAL248
|
4.2
|
18.4
|
0.3
|
|
CG1
|
A:VAL248
|
4.2
|
17.6
|
0.3
|
|
CE1
|
A:PHE291
|
4.2
|
10.8
|
0.1
|
|
N
|
A:ILE283
|
4.3
|
9.4
|
0.3
|
|
N
|
A:ILE283
|
4.3
|
9.4
|
0.3
|
|
O
|
A:PRO282
|
4.4
|
8.5
|
0.3
|
|
O
|
A:PRO282
|
4.4
|
8.5
|
0.3
|
|
CD2
|
A:PHE291
|
4.4
|
10.9
|
0.3
|
|
CD2
|
A:PHE291
|
4.4
|
10.5
|
0.1
|
|
N
|
A:ILE283
|
4.5
|
8.8
|
0.1
|
|
O
|
A:HOH565
|
4.5
|
13.7
|
0.1
|
|
O
|
A:HOH689
|
4.5
|
17.5
|
0.1
|
|
N
|
A:ILE283
|
4.5
|
9.1
|
0.3
|
|
CD2
|
A:PHE291
|
4.6
|
9.6
|
0.3
|
|
CD2
|
A:PHE291
|
4.6
|
9.6
|
0.3
|
|
CE1
|
A:PHE291
|
4.7
|
11.2
|
0.3
|
|
CE1
|
A:PHE291
|
4.7
|
11.2
|
0.3
|
|
C
|
A:PRO282
|
4.7
|
8.4
|
0.3
|
|
C
|
A:PRO282
|
4.7
|
8.3
|
0.3
|
|
CA
|
A:PHE291
|
4.8
|
9.0
|
0.1
|
|
CA
|
A:PHE291
|
4.8
|
8.7
|
0.3
|
|
CA
|
A:PHE291
|
4.8
|
8.6
|
0.3
|
|
CA
|
A:PHE291
|
4.8
|
8.6
|
0.3
|
|
CG1
|
A:ILE283
|
4.9
|
9.8
|
0.1
|
|
CG1
|
A:ILE283
|
4.9
|
11.7
|
0.3
|
|
CZ
|
A:PHE291
|
4.9
|
11.6
|
0.3
|
|
N
|
A:SER284
|
5.0
|
9.5
|
0.3
|
|
N
|
A:SER284
|
5.0
|
9.6
|
0.3
|
|
CZ
|
A:PHE291
|
5.0
|
10.8
|
0.1
|
|
O
|
A:PRO282
|
5.0
|
9.7
|
0.1
|
|
O
|
A:PRO282
|
5.0
|
9.9
|
0.3
|
|
Fluorine binding site 2 out
of 4 in 5rcf
Go back to
Fluorine Binding Sites List in 5rcf
Fluorine binding site 2 out
of 4 in the Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F401
b:11.7
occ:0.13
|
F
|
A:RE7401
|
0.0
|
11.7
|
0.1
|
|
F
|
A:RE7401
|
0.0
|
11.4
|
0.3
|
|
C5
|
A:RE7401
|
1.4
|
11.4
|
0.3
|
|
C5
|
A:RE7401
|
1.4
|
11.6
|
0.1
|
|
O4
|
A:PG4411
|
1.9
|
49.5
|
0.3
|
|
C7
|
A:PG4411
|
1.9
|
51.7
|
0.3
|
|
O4
|
A:PG4411
|
2.0
|
50.5
|
0.3
|
|
C7
|
A:PG4411
|
2.0
|
52.8
|
0.3
|
|
C6
|
A:RE7401
|
2.3
|
11.8
|
0.1
|
|
C4
|
A:RE7401
|
2.3
|
10.9
|
0.3
|
|
C6
|
A:RE7401
|
2.3
|
11.9
|
0.3
|
|
C4
|
A:RE7401
|
2.4
|
11.3
|
0.1
|
|
C6
|
A:PG4411
|
2.5
|
48.5
|
0.3
|
|
C6
|
A:PG4411
|
2.6
|
49.5
|
0.3
|
|
CA
|
A:ILE283
|
3.1
|
10.5
|
0.3
|
|
CA
|
A:ILE283
|
3.1
|
10.5
|
0.3
|
|
C8
|
A:PG4411
|
3.1
|
52.0
|
0.3
|
|
C8
|
A:PG4411
|
3.2
|
53.0
|
0.3
|
|
O
|
A:ILE283
|
3.2
|
12.6
|
0.3
|
|
O
|
A:ILE283
|
3.2
|
12.6
|
0.3
|
|
CG2
|
A:ILE283
|
3.3
|
9.8
|
0.1
|
|
CA
|
A:ILE283
|
3.3
|
8.5
|
0.1
|
|
CG2
|
A:ILE283
|
3.3
|
11.8
|
0.3
|
|
CB
|
A:ILE283
|
3.4
|
9.3
|
0.1
|
|
CA
|
A:ILE283
|
3.4
|
9.4
|
0.3
|
|
CD1
|
A:PHE291
|
3.4
|
10.9
|
0.3
|
|
O5
|
A:PG4411
|
3.4
|
52.5
|
0.3
|
|
CB
|
A:ILE283
|
3.4
|
10.8
|
0.3
|
|
O
|
A:HOH689
|
3.4
|
20.9
|
0.3
|
|
CD1
|
A:PHE291
|
3.4
|
10.4
|
0.1
|
|
C5
|
A:PG4411
|
3.4
|
48.0
|
0.3
|
|
O5
|
A:PG4411
|
3.5
|
51.4
|
0.3
|
|
C5
|
A:PG4411
|
3.5
|
48.8
|
0.3
|
|
CB
|
A:ILE283
|
3.5
|
11.6
|
0.3
|
|
CB
|
A:ILE283
|
3.5
|
11.6
|
0.3
|
|
CG
|
A:PHE291
|
3.5
|
9.8
|
0.3
|
|
CG
|
A:PHE291
|
3.6
|
9.9
|
0.1
|
|
CB
|
A:PHE291
|
3.6
|
9.6
|
0.1
|
|
C3
|
A:RE7401
|
3.6
|
11.6
|
0.3
|
|
C7
|
A:RE7401
|
3.6
|
11.7
|
0.1
|
|
C7
|
A:RE7401
|
3.6
|
11.5
|
0.3
|
|
CB
|
A:PHE291
|
3.6
|
9.4
|
0.3
|
|
C3
|
A:RE7401
|
3.6
|
11.7
|
0.1
|
|
CB
|
A:PHE291
|
3.6
|
9.8
|
0.3
|
|
CB
|
A:PHE291
|
3.6
|
9.8
|
0.3
|
|
C
|
A:ILE283
|
3.6
|
10.5
|
0.3
|
|
C
|
A:ILE283
|
3.6
|
10.5
|
0.3
|
|
CG2
|
A:ILE283
|
3.7
|
12.2
|
0.3
|
|
CG2
|
A:ILE283
|
3.7
|
12.2
|
0.3
|
|
O
|
A:HOH565
|
3.7
|
21.4
|
0.3
|
|
CG
|
A:PHE291
|
3.8
|
9.7
|
0.3
|
|
CG
|
A:PHE291
|
3.8
|
9.7
|
0.3
|
|
O
|
A:ILE283
|
3.8
|
6.8
|
0.1
|
|
O
|
A:ILE283
|
3.8
|
14.2
|
0.3
|
|
CG1
|
A:VAL248
|
3.8
|
15.9
|
0.1
|
|
CD1
|
A:PHE291
|
3.9
|
10.3
|
0.3
|
|
CD1
|
A:PHE291
|
3.9
|
10.3
|
0.3
|
|
O3
|
A:PG4411
|
4.0
|
47.6
|
0.3
|
|
O3
|
A:PG4411
|
4.0
|
48.3
|
0.3
|
|
C
|
A:ILE283
|
4.0
|
8.4
|
0.1
|
|
CG1
|
A:VAL248
|
4.1
|
16.8
|
0.3
|
|
C
|
A:ILE283
|
4.1
|
10.1
|
0.3
|
|
C2
|
A:RE7401
|
4.1
|
11.6
|
0.3
|
|
C2
|
A:RE7401
|
4.1
|
11.8
|
0.1
|
|
CE1
|
A:PHE291
|
4.2
|
11.8
|
0.3
|
|
CG1
|
A:VAL248
|
4.2
|
18.4
|
0.3
|
|
CG1
|
A:VAL248
|
4.2
|
17.6
|
0.3
|
|
CE1
|
A:PHE291
|
4.2
|
10.8
|
0.1
|
|
N
|
A:ILE283
|
4.3
|
9.4
|
0.3
|
|
N
|
A:ILE283
|
4.3
|
9.4
|
0.3
|
|
O
|
A:PRO282
|
4.3
|
8.5
|
0.3
|
|
O
|
A:PRO282
|
4.3
|
8.5
|
0.3
|
|
CD2
|
A:PHE291
|
4.4
|
10.9
|
0.3
|
|
CD2
|
A:PHE291
|
4.4
|
10.5
|
0.1
|
|
N
|
A:ILE283
|
4.5
|
8.8
|
0.1
|
|
O
|
A:HOH689
|
4.5
|
17.5
|
0.1
|
|
O
|
A:HOH565
|
4.5
|
13.7
|
0.1
|
|
N
|
A:ILE283
|
4.5
|
9.1
|
0.3
|
|
CD2
|
A:PHE291
|
4.6
|
9.6
|
0.3
|
|
CD2
|
A:PHE291
|
4.6
|
9.6
|
0.3
|
|
CE1
|
A:PHE291
|
4.7
|
11.2
|
0.3
|
|
CE1
|
A:PHE291
|
4.7
|
11.2
|
0.3
|
|
C
|
A:PRO282
|
4.7
|
8.4
|
0.3
|
|
C
|
A:PRO282
|
4.7
|
8.3
|
0.3
|
|
CA
|
A:PHE291
|
4.8
|
9.0
|
0.1
|
|
CA
|
A:PHE291
|
4.8
|
8.7
|
0.3
|
|
CA
|
A:PHE291
|
4.8
|
8.6
|
0.3
|
|
CA
|
A:PHE291
|
4.8
|
8.6
|
0.3
|
|
CG1
|
A:ILE283
|
4.9
|
9.8
|
0.1
|
|
CG1
|
A:ILE283
|
4.9
|
11.7
|
0.3
|
|
CZ
|
A:PHE291
|
4.9
|
11.6
|
0.3
|
|
N
|
A:SER284
|
5.0
|
9.5
|
0.3
|
|
N
|
A:SER284
|
5.0
|
9.6
|
0.3
|
|
O
|
A:PRO282
|
5.0
|
9.7
|
0.1
|
|
CZ
|
A:PHE291
|
5.0
|
10.8
|
0.1
|
|
O
|
A:PRO282
|
5.0
|
9.9
|
0.3
|
|
Fluorine binding site 3 out
of 4 in 5rcf
Go back to
Fluorine Binding Sites List in 5rcf
Fluorine binding site 3 out
of 4 in the Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F402
b:16.6
occ:0.28
|
F
|
A:RE7402
|
0.0
|
16.6
|
0.3
|
|
F
|
A:RE7402
|
0.0
|
15.2
|
0.1
|
|
O
|
A:HOH674
|
1.3
|
22.5
|
0.3
|
|
C5
|
A:RE7402
|
1.4
|
14.5
|
0.1
|
|
C5
|
A:RE7402
|
1.4
|
14.4
|
0.3
|
|
O
|
A:HOH674
|
1.9
|
20.0
|
0.3
|
|
C6
|
A:RE7402
|
2.3
|
14.6
|
0.3
|
|
C6
|
A:RE7402
|
2.3
|
14.3
|
0.1
|
|
C4
|
A:RE7402
|
2.3
|
15.9
|
0.1
|
|
C4
|
A:RE7402
|
2.4
|
16.1
|
0.3
|
|
O
|
A:HOH622
|
3.3
|
21.2
|
0.3
|
|
O
|
A:HOH622
|
3.3
|
20.6
|
0.3
|
|
CD2
|
A:TYR79
|
3.4
|
14.0
|
0.3
|
|
CD2
|
A:TYR79
|
3.4
|
16.1
|
0.1
|
|
O
|
A:GLY221
|
3.5
|
11.4
|
0.3
|
|
O
|
A:GLY221
|
3.5
|
11.4
|
0.3
|
|
O
|
A:GLY221
|
3.5
|
11.3
|
0.3
|
|
OD2
|
A:ASP35
|
3.6
|
11.1
|
0.3
|
|
OD2
|
A:ASP35
|
3.6
|
11.1
|
0.3
|
|
C7
|
A:RE7402
|
3.6
|
14.8
|
0.3
|
|
C7
|
A:RE7402
|
3.6
|
14.6
|
0.1
|
|
C3
|
A:RE7402
|
3.6
|
15.9
|
0.1
|
|
O
|
A:GLY221
|
3.6
|
9.9
|
0.1
|
|
C3
|
A:RE7402
|
3.6
|
16.1
|
0.3
|
|
OD2
|
A:ASP35
|
3.8
|
10.3
|
0.3
|
|
O
|
A:HOH622
|
3.8
|
11.1
|
0.3
|
|
OD2
|
A:ASP35
|
3.8
|
9.5
|
0.1
|
|
O
|
A:HOH622
|
3.8
|
10.5
|
0.1
|
|
CD2
|
A:LEU125
|
3.8
|
13.1
|
0.3
|
|
CD2
|
A:LEU125
|
3.8
|
13.0
|
0.3
|
|
CD2
|
A:TYR79
|
3.9
|
13.1
|
0.3
|
|
CD2
|
A:TYR79
|
3.9
|
13.0
|
0.3
|
|
CE2
|
A:TYR79
|
3.9
|
15.9
|
0.1
|
|
CE2
|
A:TYR79
|
3.9
|
13.8
|
0.3
|
|
CG
|
A:TYR79
|
4.0
|
14.3
|
0.3
|
|
CG
|
A:TYR79
|
4.0
|
16.4
|
0.1
|
|
CG
|
A:TYR79
|
4.0
|
14.1
|
0.3
|
|
CG
|
A:TYR79
|
4.0
|
14.1
|
0.3
|
|
C2
|
A:RE7402
|
4.1
|
15.1
|
0.1
|
|
O
|
A:HOH526
|
4.1
|
11.2
|
0.1
|
|
C2
|
A:RE7402
|
4.1
|
15.4
|
0.3
|
|
CD2
|
A:LEU125
|
4.2
|
12.5
|
0.3
|
|
CD2
|
A:LEU125
|
4.2
|
10.8
|
0.1
|
|
CG
|
A:ASP35
|
4.2
|
10.1
|
0.3
|
|
CG
|
A:ASP35
|
4.2
|
10.1
|
0.3
|
|
CB
|
A:TYR79
|
4.3
|
15.2
|
0.3
|
|
CB
|
A:TYR79
|
4.3
|
17.0
|
0.1
|
|
CE2
|
A:TYR79
|
4.3
|
11.8
|
0.3
|
|
CE2
|
A:TYR79
|
4.3
|
11.9
|
0.3
|
|
CB
|
A:TYR79
|
4.3
|
15.2
|
0.3
|
|
CB
|
A:TYR79
|
4.3
|
15.1
|
0.3
|
|
O
|
A:HOH526
|
4.3
|
11.0
|
0.3
|
|
C
|
A:GLY221
|
4.3
|
9.9
|
0.3
|
|
C
|
A:GLY221
|
4.3
|
9.9
|
0.3
|
|
C
|
A:GLY221
|
4.3
|
9.9
|
0.3
|
|
CG
|
A:ASP35
|
4.3
|
9.0
|
0.1
|
|
C
|
A:GLY221
|
4.3
|
9.5
|
0.1
|
|
CG
|
A:ASP35
|
4.4
|
9.2
|
0.3
|
|
CA
|
A:GLY221
|
4.5
|
9.5
|
0.1
|
|
CA
|
A:GLY221
|
4.5
|
9.8
|
0.3
|
|
CA
|
A:GLY221
|
4.5
|
9.8
|
0.3
|
|
CA
|
A:GLY221
|
4.5
|
9.8
|
0.3
|
|
OD1
|
A:ASP35
|
4.6
|
10.0
|
0.3
|
|
OD1
|
A:ASP35
|
4.6
|
10.0
|
0.3
|
|
O
|
A:HOH526
|
4.6
|
11.1
|
0.3
|
|
O
|
A:HOH526
|
4.6
|
11.0
|
0.3
|
|
CD1
|
A:TYR79
|
4.6
|
13.1
|
0.3
|
|
CD1
|
A:TYR79
|
4.6
|
13.1
|
0.3
|
|
OD1
|
A:ASP35
|
4.8
|
9.0
|
0.1
|
|
CZ
|
A:TYR79
|
4.8
|
15.6
|
0.1
|
|
CZ
|
A:TYR79
|
4.8
|
13.5
|
0.3
|
|
OD1
|
A:ASP35
|
4.9
|
9.0
|
0.3
|
|
CD1
|
A:TYR79
|
4.9
|
14.1
|
0.3
|
|
CD1
|
A:TYR79
|
4.9
|
16.1
|
0.1
|
|
CZ
|
A:TYR79
|
4.9
|
11.5
|
0.3
|
|
CZ
|
A:TYR79
|
4.9
|
11.5
|
0.3
|
|
Fluorine binding site 4 out
of 4 in 5rcf
Go back to
Fluorine Binding Sites List in 5rcf
Fluorine binding site 4 out
of 4 in the Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 4 of Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library H10B within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F402
b:15.2
occ:0.13
|
F
|
A:RE7402
|
0.0
|
15.2
|
0.1
|
|
F
|
A:RE7402
|
0.0
|
16.6
|
0.3
|
|
O
|
A:HOH674
|
1.3
|
22.5
|
0.3
|
|
C5
|
A:RE7402
|
1.4
|
14.5
|
0.1
|
|
C5
|
A:RE7402
|
1.4
|
14.4
|
0.3
|
|
O
|
A:HOH674
|
1.9
|
20.0
|
0.3
|
|
C6
|
A:RE7402
|
2.3
|
14.6
|
0.3
|
|
C6
|
A:RE7402
|
2.3
|
14.3
|
0.1
|
|
C4
|
A:RE7402
|
2.4
|
15.9
|
0.1
|
|
C4
|
A:RE7402
|
2.4
|
16.1
|
0.3
|
|
O
|
A:HOH622
|
3.3
|
21.2
|
0.3
|
|
O
|
A:HOH622
|
3.3
|
20.6
|
0.3
|
|
CD2
|
A:TYR79
|
3.4
|
14.0
|
0.3
|
|
CD2
|
A:TYR79
|
3.4
|
16.1
|
0.1
|
|
O
|
A:GLY221
|
3.4
|
11.4
|
0.3
|
|
O
|
A:GLY221
|
3.4
|
11.4
|
0.3
|
|
O
|
A:GLY221
|
3.5
|
11.3
|
0.3
|
|
OD2
|
A:ASP35
|
3.6
|
11.1
|
0.3
|
|
OD2
|
A:ASP35
|
3.6
|
11.1
|
0.3
|
|
O
|
A:GLY221
|
3.6
|
9.9
|
0.1
|
|
C7
|
A:RE7402
|
3.6
|
14.8
|
0.3
|
|
C7
|
A:RE7402
|
3.6
|
14.6
|
0.1
|
|
C3
|
A:RE7402
|
3.6
|
15.9
|
0.1
|
|
C3
|
A:RE7402
|
3.6
|
16.1
|
0.3
|
|
O
|
A:HOH622
|
3.8
|
11.1
|
0.3
|
|
OD2
|
A:ASP35
|
3.8
|
10.3
|
0.3
|
|
OD2
|
A:ASP35
|
3.8
|
9.5
|
0.1
|
|
O
|
A:HOH622
|
3.8
|
10.5
|
0.1
|
|
CD2
|
A:LEU125
|
3.8
|
13.1
|
0.3
|
|
CD2
|
A:LEU125
|
3.8
|
13.0
|
0.3
|
|
CD2
|
A:TYR79
|
3.9
|
13.1
|
0.3
|
|
CD2
|
A:TYR79
|
3.9
|
13.0
|
0.3
|
|
CE2
|
A:TYR79
|
3.9
|
15.9
|
0.1
|
|
CE2
|
A:TYR79
|
3.9
|
13.8
|
0.3
|
|
CG
|
A:TYR79
|
4.0
|
14.3
|
0.3
|
|
CG
|
A:TYR79
|
4.0
|
16.4
|
0.1
|
|
CG
|
A:TYR79
|
4.1
|
14.1
|
0.3
|
|
CG
|
A:TYR79
|
4.1
|
14.1
|
0.3
|
|
O
|
A:HOH526
|
4.1
|
11.2
|
0.1
|
|
C2
|
A:RE7402
|
4.1
|
15.1
|
0.1
|
|
C2
|
A:RE7402
|
4.1
|
15.4
|
0.3
|
|
CD2
|
A:LEU125
|
4.2
|
12.5
|
0.3
|
|
CD2
|
A:LEU125
|
4.2
|
10.8
|
0.1
|
|
CG
|
A:ASP35
|
4.2
|
10.1
|
0.3
|
|
CG
|
A:ASP35
|
4.2
|
10.1
|
0.3
|
|
CB
|
A:TYR79
|
4.3
|
15.2
|
0.3
|
|
O
|
A:HOH526
|
4.3
|
11.0
|
0.3
|
|
C
|
A:GLY221
|
4.3
|
9.9
|
0.3
|
|
C
|
A:GLY221
|
4.3
|
9.9
|
0.3
|
|
C
|
A:GLY221
|
4.3
|
9.9
|
0.3
|
|
CB
|
A:TYR79
|
4.3
|
17.0
|
0.1
|
|
CE2
|
A:TYR79
|
4.3
|
11.8
|
0.3
|
|
CE2
|
A:TYR79
|
4.3
|
11.9
|
0.3
|
|
CB
|
A:TYR79
|
4.3
|
15.2
|
0.3
|
|
CB
|
A:TYR79
|
4.3
|
15.1
|
0.3
|
|
C
|
A:GLY221
|
4.3
|
9.5
|
0.1
|
|
CG
|
A:ASP35
|
4.3
|
9.0
|
0.1
|
|
CG
|
A:ASP35
|
4.3
|
9.2
|
0.3
|
|
CA
|
A:GLY221
|
4.5
|
9.5
|
0.1
|
|
CA
|
A:GLY221
|
4.5
|
9.8
|
0.3
|
|
CA
|
A:GLY221
|
4.5
|
9.8
|
0.3
|
|
CA
|
A:GLY221
|
4.5
|
9.8
|
0.3
|
|
OD1
|
A:ASP35
|
4.6
|
10.0
|
0.3
|
|
OD1
|
A:ASP35
|
4.6
|
10.0
|
0.3
|
|
O
|
A:HOH526
|
4.6
|
11.1
|
0.3
|
|
O
|
A:HOH526
|
4.6
|
11.0
|
0.3
|
|
CD1
|
A:TYR79
|
4.7
|
13.1
|
0.3
|
|
CD1
|
A:TYR79
|
4.7
|
13.1
|
0.3
|
|
OD1
|
A:ASP35
|
4.8
|
9.0
|
0.1
|
|
CZ
|
A:TYR79
|
4.8
|
15.6
|
0.1
|
|
CZ
|
A:TYR79
|
4.9
|
13.5
|
0.3
|
|
OD1
|
A:ASP35
|
4.9
|
9.0
|
0.3
|
|
CD1
|
A:TYR79
|
4.9
|
14.1
|
0.3
|
|
CD1
|
A:TYR79
|
4.9
|
16.1
|
0.1
|
|
CZ
|
A:TYR79
|
4.9
|
11.5
|
0.3
|
|
CZ
|
A:TYR79
|
4.9
|
11.5
|
0.3
|
|
Reference:
J.Wollenhaupt,
A.Metz,
T.Barthel,
G.M.A.Lima,
A.Heine,
U.Mueller,
G.Klebe,
M.S.Weiss.
F2X-Universal and F2X-Entry: Structurally Diverse Compound Libraries For Crystallographic Fragment Screening. Structure 2020.
ISSN: ISSN 0969-2126
PubMed: 32413289
DOI: 10.1016/J.STR.2020.04.019
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