Thallium in PDB 1fpk: Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)
Enzymatic activity of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)
All present enzymatic activity of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm):
3.1.3.11;
Protein crystallography data
The structure of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm), PDB code: 1fpk
was solved by
V.Villeret,
W.N.Lipscomb,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
8.00 /
3.00
|
Space group
|
P 32 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
132.600,
132.600,
67.700,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
22.6 /
n/a
|
Thallium Binding Sites:
The binding sites of Thallium atom in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)
(pdb code 1fpk). This binding sites where shown within
5.0 Angstroms radius around Thallium atom.
In total 6 binding sites of Thallium where determined in the
Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm), PDB code: 1fpk:
Jump to Thallium binding site number:
1;
2;
3;
4;
5;
6;
Thallium binding site 1 out
of 6 in 1fpk
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Thallium Binding Sites List in 1fpk
Thallium binding site 1 out
of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 1 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Tl336
b:40.0
occ:0.45
|
OE2
|
A:GLU97
|
2.4
|
48.8
|
1.0
|
OE1
|
A:GLU280
|
2.6
|
37.2
|
1.0
|
OD2
|
A:ASP118
|
2.6
|
40.9
|
1.0
|
OD1
|
A:ASP121
|
2.9
|
13.2
|
1.0
|
CD
|
A:GLU280
|
3.0
|
25.9
|
1.0
|
OE2
|
A:GLU280
|
3.5
|
26.4
|
1.0
|
CG
|
A:ASP118
|
3.5
|
35.5
|
1.0
|
CD
|
A:GLU97
|
3.5
|
45.5
|
1.0
|
TL
|
A:TL338
|
3.6
|
40.0
|
0.7
|
NH1
|
A:ARG276
|
3.7
|
47.0
|
1.0
|
TL
|
A:TL337
|
3.9
|
40.0
|
0.7
|
CG
|
A:GLU280
|
3.9
|
18.9
|
1.0
|
OE1
|
A:GLU97
|
4.1
|
46.8
|
1.0
|
CG
|
A:ASP121
|
4.1
|
30.7
|
1.0
|
OD1
|
A:ASP118
|
4.2
|
39.2
|
1.0
|
CB
|
A:ASP118
|
4.4
|
23.9
|
1.0
|
CZ
|
A:ARG276
|
4.5
|
49.1
|
1.0
|
CB
|
A:ASP121
|
4.6
|
21.3
|
1.0
|
CG
|
A:GLU97
|
4.7
|
39.1
|
1.0
|
CA
|
A:ASP121
|
4.8
|
23.5
|
1.0
|
|
Thallium binding site 2 out
of 6 in 1fpk
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Thallium Binding Sites List in 1fpk
Thallium binding site 2 out
of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 2 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Tl337
b:40.0
occ:0.70
|
O
|
A:LEU120
|
2.1
|
32.1
|
1.0
|
OD1
|
A:ASP118
|
2.7
|
39.2
|
1.0
|
OE1
|
A:GLU97
|
2.8
|
46.8
|
1.0
|
C
|
A:LEU120
|
3.0
|
20.1
|
1.0
|
CA
|
A:ASP121
|
3.4
|
23.5
|
1.0
|
CG
|
A:ASP118
|
3.4
|
35.5
|
1.0
|
OD2
|
A:ASP118
|
3.4
|
40.9
|
1.0
|
N
|
A:ASP121
|
3.5
|
20.7
|
1.0
|
CD
|
A:GLU97
|
3.6
|
45.5
|
1.0
|
OE2
|
A:GLU97
|
3.7
|
48.8
|
1.0
|
TL
|
A:TL336
|
3.9
|
40.0
|
0.5
|
N
|
A:GLY122
|
4.1
|
30.5
|
1.0
|
CA
|
A:LEU120
|
4.2
|
16.4
|
1.0
|
N
|
A:LEU120
|
4.2
|
16.3
|
1.0
|
OE2
|
A:GLU98
|
4.3
|
55.2
|
1.0
|
C
|
A:ASP121
|
4.3
|
28.6
|
1.0
|
OD2
|
A:ASP74
|
4.3
|
33.9
|
1.0
|
OG
|
A:SER123
|
4.3
|
40.6
|
1.0
|
CB
|
A:ASP121
|
4.4
|
21.3
|
1.0
|
OD1
|
A:ASP121
|
4.7
|
13.2
|
1.0
|
CB
|
A:ASP118
|
4.8
|
23.9
|
1.0
|
CB
|
A:LEU120
|
4.9
|
12.8
|
1.0
|
CG
|
A:ASP121
|
5.0
|
30.7
|
1.0
|
|
Thallium binding site 3 out
of 6 in 1fpk
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Thallium Binding Sites List in 1fpk
Thallium binding site 3 out
of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 3 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Tl338
b:40.0
occ:0.67
|
OE1
|
A:GLU280
|
2.9
|
37.2
|
1.0
|
TL
|
A:TL336
|
3.6
|
40.0
|
0.5
|
NH1
|
A:ARG276
|
3.8
|
47.0
|
1.0
|
CD
|
A:GLU280
|
3.8
|
25.9
|
1.0
|
OE2
|
A:GLU280
|
4.0
|
26.4
|
1.0
|
CD2
|
A:LEU275
|
4.2
|
5.5
|
1.0
|
OD1
|
A:ASP121
|
4.2
|
13.2
|
1.0
|
CG
|
A:LEU275
|
4.2
|
7.3
|
1.0
|
CA
|
A:LEU275
|
4.5
|
17.3
|
1.0
|
CB
|
A:LEU275
|
4.6
|
12.5
|
1.0
|
CE
|
A:LYS274
|
4.7
|
34.0
|
1.0
|
CD
|
A:LYS274
|
4.7
|
26.5
|
1.0
|
NZ
|
A:LYS274
|
4.8
|
38.6
|
1.0
|
CG
|
A:LYS274
|
4.8
|
27.8
|
1.0
|
N
|
A:LEU275
|
5.0
|
22.7
|
1.0
|
|
Thallium binding site 4 out
of 6 in 1fpk
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Thallium Binding Sites List in 1fpk
Thallium binding site 4 out
of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 4 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Tl336
b:40.0
occ:0.49
|
OE1
|
B:GLU97
|
2.5
|
53.7
|
1.0
|
OE1
|
B:GLU280
|
2.6
|
55.9
|
1.0
|
OD2
|
B:ASP118
|
2.6
|
49.4
|
1.0
|
CD
|
B:GLU280
|
3.1
|
50.7
|
1.0
|
CG
|
B:ASP118
|
3.4
|
44.6
|
1.0
|
CD
|
B:GLU97
|
3.4
|
52.0
|
1.0
|
OD1
|
B:ASP121
|
3.4
|
39.9
|
1.0
|
OE2
|
B:GLU280
|
3.5
|
51.6
|
1.0
|
TL
|
B:TL338
|
3.6
|
40.0
|
0.7
|
OE2
|
B:GLU97
|
3.7
|
55.5
|
1.0
|
OD1
|
B:ASP118
|
3.8
|
49.5
|
1.0
|
TL
|
B:TL337
|
3.9
|
40.0
|
0.7
|
CG
|
B:GLU280
|
4.0
|
45.3
|
1.0
|
CB
|
B:ASP118
|
4.4
|
35.7
|
1.0
|
CG
|
B:ASP121
|
4.5
|
41.4
|
1.0
|
CB
|
B:ASP121
|
4.7
|
35.7
|
1.0
|
CG
|
B:GLU97
|
4.7
|
45.2
|
1.0
|
CA
|
B:ASP121
|
4.8
|
33.2
|
1.0
|
CB
|
B:GLU97
|
4.9
|
35.5
|
1.0
|
NE
|
B:ARG276
|
4.9
|
52.3
|
1.0
|
|
Thallium binding site 5 out
of 6 in 1fpk
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Thallium Binding Sites List in 1fpk
Thallium binding site 5 out
of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 5 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Tl337
b:40.0
occ:0.65
|
O
|
B:LEU120
|
2.2
|
45.9
|
1.0
|
OE2
|
B:GLU97
|
2.6
|
55.5
|
1.0
|
OD1
|
B:ASP118
|
2.7
|
49.5
|
1.0
|
OE2
|
B:GLU98
|
3.1
|
51.6
|
1.0
|
C
|
B:LEU120
|
3.2
|
30.8
|
1.0
|
CA
|
B:ASP121
|
3.4
|
33.2
|
1.0
|
CD
|
B:GLU97
|
3.5
|
52.0
|
1.0
|
CG
|
B:ASP118
|
3.6
|
44.6
|
1.0
|
OD2
|
B:ASP118
|
3.6
|
49.4
|
1.0
|
N
|
B:ASP121
|
3.6
|
25.3
|
1.0
|
OG
|
B:SER123
|
3.8
|
57.0
|
1.0
|
TL
|
B:TL336
|
3.9
|
40.0
|
0.5
|
OE1
|
B:GLU97
|
4.0
|
53.7
|
1.0
|
N
|
B:GLY122
|
4.1
|
38.5
|
1.0
|
CD
|
B:GLU98
|
4.1
|
53.5
|
1.0
|
C
|
B:ASP121
|
4.2
|
37.6
|
1.0
|
CA
|
B:LEU120
|
4.3
|
26.0
|
1.0
|
OE1
|
B:GLU98
|
4.3
|
53.8
|
1.0
|
N
|
B:LEU120
|
4.4
|
26.3
|
1.0
|
CG
|
B:GLU97
|
4.5
|
45.2
|
1.0
|
CB
|
B:ASP121
|
4.5
|
35.7
|
1.0
|
OD1
|
B:ASP121
|
4.9
|
39.9
|
1.0
|
N
|
B:SER123
|
4.9
|
54.5
|
1.0
|
OD2
|
B:ASP74
|
4.9
|
37.2
|
1.0
|
CB
|
B:ASP118
|
5.0
|
35.7
|
1.0
|
|
Thallium binding site 6 out
of 6 in 1fpk
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Thallium Binding Sites List in 1fpk
Thallium binding site 6 out
of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm)
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 6 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Thallium Ions (10 Mm) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Tl338
b:40.0
occ:0.68
|
OE1
|
B:GLU280
|
2.9
|
55.9
|
1.0
|
TL
|
B:TL336
|
3.6
|
40.0
|
0.5
|
CD
|
B:GLU280
|
3.8
|
50.7
|
1.0
|
OE2
|
B:GLU280
|
3.8
|
51.6
|
1.0
|
OD1
|
B:ASP121
|
4.2
|
39.9
|
1.0
|
CE
|
B:LYS274
|
4.5
|
28.6
|
1.0
|
CG
|
B:LEU275
|
4.6
|
29.6
|
1.0
|
CD2
|
B:LEU275
|
4.6
|
24.5
|
1.0
|
CA
|
B:LEU275
|
4.7
|
30.6
|
1.0
|
CG
|
B:LYS274
|
4.8
|
21.3
|
1.0
|
CD
|
B:LYS274
|
4.8
|
24.2
|
1.0
|
CB
|
B:LEU275
|
4.8
|
27.5
|
1.0
|
|
Reference:
V.Villeret,
S.Huang,
H.J.Fromm,
W.N.Lipscomb.
Crystallographic Evidence For the Action of Potassium, Thallium, and Lithium Ions on Fructose-1,6-Bisphosphatase. Proc.Natl.Acad.Sci.Usa V. 92 8916 1995.
ISSN: ISSN 0027-8424
PubMed: 7568043
DOI: 10.1073/PNAS.92.19.8916
Page generated: Wed Dec 16 02:28:32 2020
|