Fluorine in PDB 5fwg: Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase
Enzymatic activity of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase
All present enzymatic activity of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase:
2.5.1.18;
Protein crystallography data
The structure of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase, PDB code: 5fwg
was solved by
J.F.Parsons,
G.Xiao,
R.N.Armstrong,
G.L.Gilliland,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
65.00 /
2.00
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
86.939,
68.747,
80.539,
90.00,
105.08,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase
(pdb code 5fwg). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 8 binding sites of Fluorine where determined in the
Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase, PDB code: 5fwg:
Jump to Fluorine binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Fluorine binding site 1 out
of 8 in 5fwg
Go back to
Fluorine Binding Sites List in 5fwg
Fluorine binding site 1 out
of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F7
b:37.0
occ:1.00
|
F
|
A:FTR7
|
0.0
|
37.0
|
1.0
|
CZ3
|
A:FTR7
|
1.3
|
80.8
|
1.0
|
CE3
|
A:FTR7
|
2.3
|
19.2
|
1.0
|
CH2
|
A:FTR7
|
2.4
|
22.6
|
1.0
|
CA
|
A:MET34
|
3.5
|
38.5
|
1.0
|
CB
|
A:MET34
|
3.5
|
38.3
|
1.0
|
N
|
A:MET34
|
3.6
|
39.1
|
1.0
|
CD2
|
A:FTR7
|
3.6
|
48.9
|
1.0
|
CZ2
|
A:FTR7
|
3.6
|
0.0
|
1.0
|
C
|
A:ALA33
|
3.7
|
39.0
|
1.0
|
O
|
A:ALA33
|
3.7
|
44.5
|
1.0
|
CG
|
A:ARG42
|
3.8
|
42.0
|
1.0
|
CA
|
A:ARG42
|
3.9
|
30.3
|
1.0
|
CE2
|
A:FTR7
|
4.1
|
30.6
|
1.0
|
O
|
A:ARG42
|
4.1
|
24.9
|
1.0
|
CB
|
A:TYR32
|
4.2
|
20.3
|
1.0
|
CB
|
A:ARG42
|
4.2
|
32.1
|
1.0
|
C
|
A:ARG42
|
4.3
|
23.8
|
1.0
|
CB
|
A:FTR45
|
4.3
|
19.9
|
1.0
|
N
|
A:ALA33
|
4.3
|
32.8
|
1.0
|
O
|
A:ASP41
|
4.4
|
48.9
|
1.0
|
C
|
A:TYR32
|
4.5
|
29.7
|
1.0
|
CA
|
A:ALA33
|
4.5
|
29.6
|
1.0
|
CE
|
A:MET34
|
4.6
|
38.6
|
1.0
|
N
|
A:FTR45
|
4.6
|
20.4
|
1.0
|
O
|
A:TYR32
|
4.7
|
41.8
|
1.0
|
CG
|
A:MET34
|
4.7
|
44.2
|
1.0
|
C
|
A:MET34
|
4.9
|
34.6
|
1.0
|
CG
|
A:FTR7
|
4.9
|
48.5
|
1.0
|
O
|
A:HOH826
|
4.9
|
22.8
|
0.9
|
CA
|
A:TYR32
|
5.0
|
17.6
|
1.0
|
|
Fluorine binding site 2 out
of 8 in 5fwg
Go back to
Fluorine Binding Sites List in 5fwg
Fluorine binding site 2 out
of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F45
b:37.0
occ:1.00
|
F
|
A:FTR45
|
0.0
|
37.0
|
1.0
|
CZ3
|
A:FTR45
|
1.3
|
30.8
|
1.0
|
CE3
|
A:FTR45
|
2.3
|
18.3
|
1.0
|
CH2
|
A:FTR45
|
2.3
|
19.6
|
1.0
|
CE2
|
A:TYR61
|
3.0
|
20.4
|
1.0
|
CD1
|
A:LEU52
|
3.0
|
46.1
|
1.0
|
CD2
|
A:TYR61
|
3.5
|
21.5
|
1.0
|
CD2
|
A:FTR45
|
3.6
|
20.9
|
1.0
|
CZ2
|
A:FTR45
|
3.6
|
27.9
|
1.0
|
OH
|
A:TYR32
|
3.7
|
36.0
|
1.0
|
CZ
|
A:TYR61
|
4.0
|
7.8
|
1.0
|
CZ
|
A:TYR32
|
4.0
|
33.3
|
1.0
|
CE2
|
A:FTR45
|
4.0
|
12.7
|
1.0
|
CD2
|
A:LEU59
|
4.1
|
27.6
|
1.0
|
CE2
|
A:TYR32
|
4.1
|
32.2
|
1.0
|
CA
|
A:LYS49
|
4.2
|
19.2
|
1.0
|
N
|
A:LYS49
|
4.3
|
20.6
|
1.0
|
O
|
A:GLU48
|
4.3
|
17.0
|
1.0
|
OH
|
A:TYR61
|
4.3
|
39.8
|
1.0
|
CG
|
A:LEU52
|
4.4
|
38.5
|
1.0
|
C
|
A:GLU48
|
4.4
|
17.3
|
1.0
|
O
|
A:FTR45
|
4.6
|
26.7
|
1.0
|
CD1
|
A:LEU54
|
4.6
|
25.8
|
1.0
|
CG
|
A:TYR61
|
4.7
|
19.8
|
1.0
|
O
|
A:LYS49
|
4.7
|
17.4
|
1.0
|
CB
|
A:GLU48
|
4.8
|
19.6
|
1.0
|
O
|
A:ASN58
|
4.8
|
16.6
|
1.0
|
CG
|
A:FTR45
|
4.9
|
23.5
|
1.0
|
C
|
A:LYS49
|
4.9
|
29.1
|
1.0
|
CE1
|
A:TYR32
|
4.9
|
25.4
|
1.0
|
CG
|
A:LYS49
|
5.0
|
34.9
|
1.0
|
CB
|
A:LYS49
|
5.0
|
16.1
|
1.0
|
|
Fluorine binding site 3 out
of 8 in 5fwg
Go back to
Fluorine Binding Sites List in 5fwg
Fluorine binding site 3 out
of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F146
b:51.4
occ:1.00
|
F
|
A:FTR146
|
0.0
|
51.4
|
1.0
|
CZ3
|
A:FTR146
|
1.4
|
74.5
|
1.0
|
CH2
|
A:FTR146
|
2.4
|
24.1
|
1.0
|
CE3
|
A:FTR146
|
2.4
|
20.7
|
1.0
|
CE1
|
A:PHE183
|
3.2
|
27.9
|
1.0
|
CA
|
A:PHE187
|
3.4
|
25.3
|
1.0
|
CB
|
A:PHE187
|
3.5
|
17.7
|
1.0
|
CZ2
|
A:FTR146
|
3.6
|
24.7
|
1.0
|
CD1
|
A:PHE187
|
3.6
|
28.3
|
1.0
|
CD2
|
A:FTR146
|
3.6
|
36.9
|
1.0
|
N
|
A:PHE187
|
3.7
|
19.5
|
1.0
|
CD1
|
A:PHE183
|
3.7
|
19.6
|
1.0
|
CZ
|
A:PHE183
|
4.0
|
15.6
|
1.0
|
CG
|
A:PHE187
|
4.0
|
25.2
|
1.0
|
CE2
|
A:FTR146
|
4.1
|
37.7
|
1.0
|
CD1
|
A:LEU190
|
4.1
|
41.9
|
1.0
|
O
|
A:PHE183
|
4.2
|
24.1
|
1.0
|
CB
|
A:ASP156
|
4.3
|
19.4
|
1.0
|
C
|
A:ARG186
|
4.4
|
31.9
|
1.0
|
CG
|
A:ASP156
|
4.5
|
18.0
|
1.0
|
OD2
|
A:ASP156
|
4.7
|
27.9
|
1.0
|
CB
|
A:ARG186
|
4.7
|
35.1
|
1.0
|
NE
|
A:ARG186
|
4.8
|
27.7
|
1.0
|
CE1
|
A:PHE187
|
4.8
|
26.1
|
1.0
|
O
|
A:ARG186
|
4.8
|
30.4
|
1.0
|
C
|
A:PHE187
|
4.8
|
32.3
|
1.0
|
CG
|
A:PHE183
|
4.9
|
17.8
|
1.0
|
CG
|
A:FTR146
|
5.0
|
21.0
|
1.0
|
|
Fluorine binding site 4 out
of 8 in 5fwg
Go back to
Fluorine Binding Sites List in 5fwg
Fluorine binding site 4 out
of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 4 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F214
b:39.7
occ:1.00
|
F
|
A:FTR214
|
0.0
|
39.7
|
1.0
|
CZ3
|
A:FTR214
|
1.3
|
23.3
|
1.0
|
CE3
|
A:FTR214
|
2.4
|
0.0
|
1.0
|
CH2
|
A:FTR214
|
2.4
|
45.1
|
1.0
|
CD1
|
A:ILE207
|
3.0
|
69.0
|
1.0
|
CE2
|
A:PHE208
|
3.0
|
68.7
|
1.0
|
CG1
|
A:ILE207
|
3.2
|
40.9
|
1.0
|
CD2
|
A:LEU110
|
3.4
|
26.9
|
1.0
|
CD2
|
A:FTR214
|
3.6
|
38.1
|
1.0
|
CZ2
|
A:FTR214
|
3.6
|
26.1
|
1.0
|
CZ
|
A:PHE208
|
3.7
|
62.2
|
1.0
|
CD2
|
A:PHE208
|
3.7
|
67.0
|
1.0
|
CE2
|
A:FTR214
|
4.1
|
30.7
|
1.0
|
CG
|
A:LEU110
|
4.1
|
34.8
|
1.0
|
CB
|
A:SER215
|
4.4
|
32.5
|
1.0
|
CB
|
A:ILE207
|
4.5
|
38.6
|
1.0
|
SG
|
A:CYS114
|
4.6
|
36.1
|
1.0
|
CD1
|
A:LEU110
|
4.7
|
32.1
|
1.0
|
NE2
|
A:GLN165
|
4.7
|
24.8
|
1.0
|
CD1
|
A:PHE169
|
4.8
|
23.9
|
1.0
|
CE1
|
A:PHE208
|
4.8
|
58.4
|
1.0
|
O
|
A:GLN165
|
4.9
|
34.9
|
1.0
|
CG
|
A:PHE208
|
4.9
|
55.8
|
1.0
|
CB
|
A:GLN165
|
4.9
|
19.3
|
1.0
|
CG
|
A:FTR214
|
4.9
|
24.3
|
1.0
|
OG
|
A:SER215
|
5.0
|
37.1
|
1.0
|
|
Fluorine binding site 5 out
of 8 in 5fwg
Go back to
Fluorine Binding Sites List in 5fwg
Fluorine binding site 5 out
of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 5 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F7
b:23.0
occ:1.00
|
F
|
B:FTR7
|
0.0
|
23.0
|
1.0
|
CZ3
|
B:FTR7
|
1.3
|
23.4
|
1.0
|
CE3
|
B:FTR7
|
2.3
|
20.8
|
1.0
|
CH2
|
B:FTR7
|
2.4
|
45.4
|
1.0
|
C
|
B:ALA33
|
3.4
|
22.4
|
1.0
|
CB
|
B:TYR32
|
3.5
|
34.2
|
1.0
|
N
|
B:MET34
|
3.5
|
30.1
|
1.0
|
CZ2
|
B:FTR7
|
3.6
|
71.4
|
1.0
|
CD2
|
B:FTR7
|
3.6
|
40.9
|
1.0
|
O
|
B:ALA33
|
3.7
|
31.4
|
1.0
|
N
|
B:ALA33
|
3.7
|
22.8
|
1.0
|
C
|
B:TYR32
|
3.9
|
40.2
|
1.0
|
CG
|
B:MET34
|
3.9
|
47.1
|
1.0
|
CA
|
B:MET34
|
3.9
|
31.9
|
1.0
|
CA
|
B:ALA33
|
3.9
|
22.0
|
1.0
|
O
|
B:TYR32
|
4.0
|
30.1
|
1.0
|
CE2
|
B:FTR7
|
4.1
|
25.5
|
1.0
|
O
|
B:HOH565
|
4.1
|
22.5
|
0.8
|
CA
|
B:ARG42
|
4.1
|
41.8
|
1.0
|
O
|
B:ARG42
|
4.2
|
26.1
|
1.0
|
CB
|
B:FTR45
|
4.2
|
40.7
|
1.0
|
CB
|
B:MET34
|
4.4
|
34.3
|
1.0
|
OD1
|
B:ASN8
|
4.4
|
86.7
|
1.0
|
O
|
B:ASP41
|
4.4
|
28.5
|
1.0
|
CA
|
B:TYR32
|
4.4
|
35.1
|
1.0
|
C
|
B:ARG42
|
4.5
|
26.8
|
1.0
|
N
|
B:FTR45
|
4.6
|
23.8
|
1.0
|
CB
|
B:ARG42
|
4.6
|
46.8
|
1.0
|
CG
|
B:TYR32
|
4.6
|
28.1
|
1.0
|
CG
|
B:ARG42
|
4.7
|
43.9
|
1.0
|
CB
|
B:GLN44
|
4.8
|
41.3
|
1.0
|
CG
|
B:FTR7
|
5.0
|
79.5
|
1.0
|
|
Fluorine binding site 6 out
of 8 in 5fwg
Go back to
Fluorine Binding Sites List in 5fwg
Fluorine binding site 6 out
of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 6 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F45
b:38.0
occ:1.00
|
F
|
B:FTR45
|
0.0
|
38.0
|
1.0
|
CZ3
|
B:FTR45
|
1.3
|
14.8
|
1.0
|
CE3
|
B:FTR45
|
2.3
|
20.1
|
1.0
|
CH2
|
B:FTR45
|
2.3
|
18.5
|
1.0
|
CE2
|
B:TYR61
|
3.0
|
17.4
|
1.0
|
CD1
|
B:LEU52
|
3.0
|
31.0
|
1.0
|
OH
|
B:TYR32
|
3.5
|
22.8
|
1.0
|
CD2
|
B:TYR61
|
3.5
|
11.1
|
1.0
|
CZ2
|
B:FTR45
|
3.6
|
34.3
|
1.0
|
CD2
|
B:FTR45
|
3.6
|
22.1
|
1.0
|
CZ
|
B:TYR61
|
4.0
|
38.7
|
1.0
|
CE2
|
B:FTR45
|
4.0
|
20.9
|
1.0
|
CZ
|
B:TYR32
|
4.1
|
30.9
|
1.0
|
CA
|
B:LYS49
|
4.2
|
21.8
|
1.0
|
CD1
|
B:LEU54
|
4.2
|
13.2
|
1.0
|
CG
|
B:LEU52
|
4.3
|
33.5
|
1.0
|
CD2
|
B:LEU59
|
4.3
|
14.7
|
1.0
|
CG
|
B:GLU48
|
4.3
|
29.4
|
1.0
|
OH
|
B:TYR61
|
4.3
|
26.3
|
1.0
|
O
|
B:GLU48
|
4.4
|
15.9
|
1.0
|
N
|
B:LYS49
|
4.5
|
20.2
|
1.0
|
C
|
B:GLU48
|
4.5
|
15.4
|
1.0
|
OE2
|
B:GLU48
|
4.6
|
30.4
|
1.0
|
CE1
|
B:TYR32
|
4.6
|
12.9
|
1.0
|
O
|
B:FTR45
|
4.7
|
20.9
|
1.0
|
O
|
B:LYS49
|
4.7
|
18.7
|
1.0
|
CG
|
B:TYR61
|
4.8
|
12.7
|
1.0
|
CE2
|
B:TYR32
|
4.9
|
17.0
|
1.0
|
C
|
B:LYS49
|
4.9
|
20.5
|
1.0
|
CB
|
B:LEU52
|
4.9
|
27.3
|
1.0
|
CG
|
B:FTR45
|
4.9
|
14.6
|
1.0
|
|
Fluorine binding site 7 out
of 8 in 5fwg
Go back to
Fluorine Binding Sites List in 5fwg
Fluorine binding site 7 out
of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 7 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F146
b:33.7
occ:1.00
|
F
|
B:FTR146
|
0.0
|
33.7
|
1.0
|
CZ3
|
B:FTR146
|
1.3
|
31.9
|
1.0
|
CE3
|
B:FTR146
|
2.3
|
30.2
|
1.0
|
CH2
|
B:FTR146
|
2.4
|
15.7
|
1.0
|
CE1
|
B:PHE183
|
3.1
|
17.7
|
1.0
|
CD1
|
B:PHE187
|
3.1
|
30.9
|
1.0
|
CB
|
B:PHE187
|
3.3
|
22.1
|
1.0
|
CA
|
B:PHE187
|
3.4
|
17.5
|
1.0
|
CZ
|
B:PHE183
|
3.5
|
14.1
|
1.0
|
CD2
|
B:FTR146
|
3.6
|
16.0
|
1.0
|
CZ2
|
B:FTR146
|
3.6
|
16.2
|
1.0
|
CG
|
B:PHE187
|
3.6
|
35.1
|
1.0
|
CD1
|
B:PHE183
|
3.8
|
23.2
|
1.0
|
CD2
|
B:LEU190
|
3.8
|
39.4
|
1.0
|
N
|
B:PHE187
|
3.9
|
18.8
|
1.0
|
CB
|
B:ASP156
|
4.1
|
26.2
|
1.0
|
CE2
|
B:FTR146
|
4.1
|
17.0
|
1.0
|
CE1
|
B:PHE187
|
4.2
|
23.0
|
1.0
|
O
|
B:PHE183
|
4.4
|
24.0
|
1.0
|
CG
|
B:ASP156
|
4.4
|
26.8
|
1.0
|
CE2
|
B:PHE183
|
4.5
|
18.8
|
1.0
|
C
|
B:ARG186
|
4.5
|
35.7
|
1.0
|
OD1
|
B:ASP156
|
4.6
|
25.6
|
1.0
|
CG
|
B:PHE183
|
4.7
|
18.3
|
1.0
|
C
|
B:PHE187
|
4.7
|
34.8
|
1.0
|
O
|
B:ARG186
|
4.7
|
40.6
|
1.0
|
CG
|
B:FTR146
|
4.9
|
18.2
|
1.0
|
CD2
|
B:PHE183
|
4.9
|
21.4
|
1.0
|
|
Fluorine binding site 8 out
of 8 in 5fwg
Go back to
Fluorine Binding Sites List in 5fwg
Fluorine binding site 8 out
of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 8 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F214
b:61.0
occ:1.00
|
F
|
B:FTR214
|
0.0
|
61.0
|
1.0
|
CZ3
|
B:FTR214
|
1.3
|
22.3
|
1.0
|
CH2
|
B:FTR214
|
2.3
|
45.6
|
1.0
|
CE3
|
B:FTR214
|
2.4
|
15.4
|
1.0
|
CE2
|
B:PHE208
|
3.2
|
36.8
|
1.0
|
CD1
|
B:ILE207
|
3.3
|
52.5
|
1.0
|
CZ2
|
B:FTR214
|
3.6
|
43.2
|
1.0
|
CD2
|
B:LEU110
|
3.6
|
31.3
|
1.0
|
CD2
|
B:FTR214
|
3.7
|
22.8
|
1.0
|
CB
|
B:SER215
|
3.7
|
61.3
|
1.0
|
CZ
|
B:PHE208
|
3.9
|
38.9
|
1.0
|
OG
|
B:SER215
|
4.0
|
59.1
|
1.0
|
CD1
|
B:LEU110
|
4.0
|
43.9
|
1.0
|
CE2
|
B:FTR214
|
4.1
|
53.6
|
1.0
|
CG
|
B:LEU110
|
4.1
|
43.8
|
1.0
|
CD2
|
B:PHE208
|
4.1
|
44.5
|
1.0
|
CD1
|
B:PHE169
|
4.3
|
48.2
|
1.0
|
CB
|
B:GLN165
|
4.4
|
34.7
|
1.0
|
CB
|
B:ILE207
|
4.4
|
37.2
|
1.0
|
CG1
|
B:ILE207
|
4.4
|
40.2
|
1.0
|
CG2
|
B:ILE207
|
4.5
|
26.1
|
1.0
|
SG
|
B:CYS114
|
4.6
|
37.3
|
1.0
|
O
|
B:GLN165
|
4.6
|
36.5
|
1.0
|
OE1
|
B:GLN165
|
4.7
|
49.1
|
1.0
|
CB
|
B:PHE169
|
5.0
|
21.3
|
1.0
|
CE1
|
B:PHE169
|
5.0
|
42.7
|
1.0
|
|
Reference:
J.F.Parsons,
G.Xiao,
G.L.Gilliland,
R.N.Armstrong.
Enzymes Harboring Unnatural Amino Acids: Mechanistic and Structural Analysis of the Enhanced Catalytic Activity of A Glutathione Transferase Containing 5-Fluorotryptophan. Biochemistry V. 37 6286 1998.
ISSN: ISSN 0006-2960
PubMed: 9572843
DOI: 10.1021/BI980219E
Page generated: Thu Aug 1 09:29:17 2024
|