Potassium in PDB 1fpi: Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm)
Enzymatic activity of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm)
All present enzymatic activity of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm):
3.1.3.11;
Protein crystallography data
The structure of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm), PDB code: 1fpi
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 /
2.30
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
61.200,
167.100,
80.000,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.9 /
n/a
|
Potassium Binding Sites:
The binding sites of Potassium atom in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm)
(pdb code 1fpi). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 6 binding sites of Potassium where determined in the
Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm), PDB code: 1fpi:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
Potassium binding site 1 out
of 6 in 1fpi
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Potassium Binding Sites List in 1fpi
Potassium binding site 1 out
of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K336
b:43.7
occ:0.40
|
O
|
A:LEU120
|
2.9
|
22.1
|
1.0
|
OE2
|
A:GLU97
|
2.9
|
56.3
|
1.0
|
OE2
|
A:GLU98
|
2.9
|
39.3
|
1.0
|
OD1
|
A:ASP118
|
3.1
|
21.8
|
1.0
|
OG
|
A:SER123
|
3.4
|
39.0
|
1.0
|
CD
|
A:GLU97
|
3.6
|
51.0
|
1.0
|
K
|
A:K337
|
3.8
|
45.7
|
0.8
|
C
|
A:LEU120
|
3.8
|
18.9
|
1.0
|
CG
|
A:ASP118
|
4.1
|
22.2
|
1.0
|
CD
|
A:GLU98
|
4.1
|
35.0
|
1.0
|
OE1
|
A:GLU97
|
4.1
|
54.0
|
1.0
|
O3P
|
A:AHG340
|
4.2
|
47.6
|
1.0
|
OD2
|
A:ASP118
|
4.3
|
24.6
|
1.0
|
CA
|
A:ASP121
|
4.5
|
22.0
|
1.0
|
CG
|
A:GLU97
|
4.5
|
43.0
|
1.0
|
N
|
A:ASP121
|
4.5
|
20.6
|
1.0
|
CB
|
A:SER123
|
4.5
|
33.9
|
1.0
|
N
|
A:LEU120
|
4.6
|
16.0
|
1.0
|
CA
|
A:LEU120
|
4.7
|
18.1
|
1.0
|
CB
|
A:GLU97
|
4.8
|
33.0
|
1.0
|
OE1
|
A:GLU98
|
4.9
|
34.6
|
1.0
|
CG
|
A:GLU98
|
4.9
|
33.9
|
1.0
|
|
Potassium binding site 2 out
of 6 in 1fpi
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Potassium Binding Sites List in 1fpi
Potassium binding site 2 out
of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K337
b:45.7
occ:0.76
|
O3P
|
A:AHG340
|
2.6
|
47.6
|
1.0
|
OE1
|
A:GLU97
|
2.7
|
54.0
|
1.0
|
OD1
|
A:ASP121
|
2.8
|
30.9
|
1.0
|
OE2
|
A:GLU280
|
2.9
|
21.9
|
1.0
|
OE2
|
A:GLU97
|
3.0
|
56.3
|
1.0
|
OD2
|
A:ASP118
|
3.0
|
24.6
|
1.0
|
CD
|
A:GLU97
|
3.2
|
51.0
|
1.0
|
O2P
|
A:AHG340
|
3.3
|
47.1
|
1.0
|
K
|
A:K338
|
3.3
|
39.2
|
0.6
|
P1
|
A:AHG340
|
3.4
|
48.2
|
1.0
|
O1
|
A:AHG340
|
3.8
|
41.6
|
1.0
|
K
|
A:K336
|
3.8
|
43.7
|
0.4
|
CG
|
A:ASP118
|
3.9
|
22.2
|
1.0
|
CG
|
A:ASP121
|
3.9
|
32.2
|
1.0
|
C1
|
A:AHG340
|
3.9
|
31.6
|
1.0
|
OD1
|
A:ASP118
|
4.0
|
21.8
|
1.0
|
CD
|
A:GLU280
|
4.1
|
20.8
|
1.0
|
CA
|
A:ASP121
|
4.2
|
22.0
|
1.0
|
CB
|
A:ASP121
|
4.4
|
25.6
|
1.0
|
N
|
A:GLY122
|
4.5
|
21.6
|
1.0
|
CG
|
A:GLU97
|
4.7
|
43.0
|
1.0
|
C2
|
A:AHG340
|
4.7
|
28.1
|
1.0
|
OE1
|
A:GLU280
|
4.7
|
24.9
|
1.0
|
O1P
|
A:AHG340
|
4.7
|
44.2
|
1.0
|
OD2
|
A:ASP121
|
4.9
|
36.0
|
1.0
|
C
|
A:ASP121
|
4.9
|
22.1
|
1.0
|
O
|
A:LEU120
|
5.0
|
22.1
|
1.0
|
|
Potassium binding site 3 out
of 6 in 1fpi
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Potassium Binding Sites List in 1fpi
Potassium binding site 3 out
of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K338
b:39.2
occ:0.60
|
OE1
|
A:GLU280
|
3.2
|
24.9
|
1.0
|
OE2
|
A:GLU280
|
3.3
|
21.9
|
1.0
|
NH1
|
A:ARG276
|
3.3
|
45.3
|
1.0
|
K
|
A:K337
|
3.3
|
45.7
|
0.8
|
CD
|
A:GLU280
|
3.6
|
20.8
|
1.0
|
OE1
|
A:GLU97
|
3.8
|
54.0
|
1.0
|
O2P
|
A:AHG340
|
4.0
|
47.1
|
1.0
|
O
|
A:LYS274
|
4.0
|
18.3
|
1.0
|
CD
|
A:ARG276
|
4.1
|
24.9
|
1.0
|
CD
|
A:GLU97
|
4.3
|
51.0
|
1.0
|
O1
|
A:AHG340
|
4.4
|
41.6
|
1.0
|
CZ
|
A:ARG276
|
4.4
|
40.0
|
1.0
|
OE2
|
A:GLU97
|
4.5
|
56.3
|
1.0
|
CD2
|
A:LEU275
|
4.6
|
16.9
|
1.0
|
CA
|
A:LEU275
|
4.6
|
17.1
|
1.0
|
N
|
A:ARG276
|
4.6
|
19.2
|
1.0
|
NE
|
A:ARG276
|
4.7
|
34.7
|
1.0
|
P1
|
A:AHG340
|
4.7
|
48.2
|
1.0
|
NH1
|
A:ARG313
|
4.7
|
31.7
|
1.0
|
C2
|
A:AHG340
|
4.7
|
28.1
|
1.0
|
C
|
A:LYS274
|
4.8
|
18.3
|
1.0
|
CG
|
A:LYS274
|
4.8
|
16.2
|
1.0
|
C1
|
A:AHG340
|
4.8
|
31.6
|
1.0
|
CE
|
A:LYS274
|
4.9
|
15.2
|
1.0
|
OD1
|
A:ASP121
|
4.9
|
30.9
|
1.0
|
O3P
|
A:AHG340
|
5.0
|
47.6
|
1.0
|
|
Potassium binding site 4 out
of 6 in 1fpi
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Potassium Binding Sites List in 1fpi
Potassium binding site 4 out
of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K336
b:42.6
occ:0.45
|
O1P
|
B:AHG340
|
2.7
|
36.8
|
1.0
|
OD1
|
B:ASP121
|
2.8
|
31.1
|
1.0
|
OE2
|
B:GLU97
|
2.8
|
46.5
|
1.0
|
OE1
|
B:GLU97
|
2.8
|
47.4
|
1.0
|
OE2
|
B:GLU280
|
2.9
|
26.4
|
1.0
|
OD2
|
B:ASP118
|
3.0
|
22.7
|
1.0
|
CD
|
B:GLU97
|
3.2
|
42.2
|
1.0
|
K
|
B:K338
|
3.5
|
40.8
|
0.6
|
P1
|
B:AHG340
|
3.5
|
43.4
|
1.0
|
O3P
|
B:AHG340
|
3.6
|
41.7
|
1.0
|
K
|
B:K337
|
3.7
|
41.7
|
0.7
|
O1
|
B:AHG340
|
3.8
|
32.5
|
1.0
|
CG
|
B:ASP118
|
3.8
|
18.2
|
1.0
|
CG
|
B:ASP121
|
3.8
|
30.0
|
1.0
|
OD1
|
B:ASP118
|
3.8
|
21.0
|
1.0
|
C1
|
B:AHG340
|
4.0
|
25.3
|
1.0
|
CD
|
B:GLU280
|
4.1
|
22.1
|
1.0
|
CA
|
B:ASP121
|
4.1
|
20.3
|
1.0
|
CB
|
B:ASP121
|
4.2
|
25.2
|
1.0
|
N
|
B:GLY122
|
4.4
|
22.1
|
1.0
|
CG
|
B:GLU97
|
4.7
|
39.4
|
1.0
|
C2
|
B:AHG340
|
4.7
|
21.5
|
1.0
|
OE1
|
B:GLU280
|
4.7
|
27.9
|
1.0
|
C
|
B:ASP121
|
4.8
|
20.9
|
1.0
|
O2P
|
B:AHG340
|
4.9
|
40.5
|
1.0
|
OD2
|
B:ASP121
|
4.9
|
31.2
|
1.0
|
O
|
B:LEU120
|
5.0
|
17.8
|
1.0
|
|
Potassium binding site 5 out
of 6 in 1fpi
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Potassium Binding Sites List in 1fpi
Potassium binding site 5 out
of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K337
b:41.7
occ:0.65
|
O
|
B:LEU120
|
2.9
|
17.8
|
1.0
|
OD1
|
B:ASP118
|
3.0
|
21.0
|
1.0
|
OE2
|
B:GLU98
|
3.1
|
56.0
|
1.0
|
OE2
|
B:GLU97
|
3.2
|
46.5
|
1.0
|
CD
|
B:GLU97
|
3.7
|
42.2
|
1.0
|
K
|
B:K336
|
3.7
|
42.6
|
0.5
|
C
|
B:LEU120
|
3.8
|
17.6
|
1.0
|
CG
|
B:ASP118
|
4.1
|
18.2
|
1.0
|
OE1
|
B:GLU97
|
4.1
|
47.4
|
1.0
|
O1P
|
B:AHG340
|
4.1
|
36.8
|
1.0
|
OG
|
B:SER123
|
4.2
|
39.4
|
1.0
|
CD
|
B:GLU98
|
4.3
|
50.4
|
1.0
|
OD2
|
B:ASP118
|
4.4
|
22.7
|
1.0
|
CG
|
B:GLU97
|
4.4
|
39.4
|
1.0
|
CA
|
B:ASP121
|
4.5
|
20.3
|
1.0
|
N
|
B:ASP121
|
4.5
|
18.4
|
1.0
|
N
|
B:LEU120
|
4.5
|
17.5
|
1.0
|
CB
|
B:GLU97
|
4.6
|
31.8
|
1.0
|
CA
|
B:LEU120
|
4.7
|
17.5
|
1.0
|
CB
|
B:SER123
|
4.8
|
36.4
|
1.0
|
CG
|
B:PRO119
|
4.9
|
14.8
|
1.0
|
|
Potassium binding site 6 out
of 6 in 1fpi
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Potassium Binding Sites List in 1fpi
Potassium binding site 6 out
of 6 in the Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1- Phosphohydrolase) Complexed with Amp, 2,5-Anhydro-D-Glucitol-1,6- Bisphosphate and Potassium Ions (100 Mm) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K338
b:40.8
occ:0.59
|
NH1
|
B:ARG276
|
3.0
|
44.9
|
1.0
|
OE2
|
B:GLU280
|
3.1
|
26.4
|
1.0
|
OE1
|
B:GLU280
|
3.3
|
27.9
|
1.0
|
K
|
B:K336
|
3.5
|
42.6
|
0.5
|
CD
|
B:GLU280
|
3.6
|
22.1
|
1.0
|
OE1
|
B:GLU97
|
3.9
|
47.4
|
1.0
|
O3P
|
B:AHG340
|
4.0
|
41.7
|
1.0
|
OE2
|
B:GLU97
|
4.0
|
46.5
|
1.0
|
O
|
B:LYS274
|
4.1
|
23.9
|
1.0
|
O1
|
B:AHG340
|
4.2
|
32.5
|
1.0
|
CD
|
B:ARG276
|
4.2
|
31.1
|
1.0
|
CZ
|
B:ARG276
|
4.2
|
44.6
|
1.0
|
CD
|
B:GLU97
|
4.2
|
42.2
|
1.0
|
CD2
|
B:LEU275
|
4.4
|
9.3
|
1.0
|
CA
|
B:LEU275
|
4.5
|
17.9
|
1.0
|
C2
|
B:AHG340
|
4.6
|
21.5
|
1.0
|
P1
|
B:AHG340
|
4.6
|
43.4
|
1.0
|
CG
|
B:LYS274
|
4.6
|
23.4
|
1.0
|
CE
|
B:LYS274
|
4.6
|
24.5
|
1.0
|
NE
|
B:ARG276
|
4.7
|
39.6
|
1.0
|
N
|
B:ARG276
|
4.7
|
19.1
|
1.0
|
C
|
B:LYS274
|
4.8
|
22.2
|
1.0
|
C1
|
B:AHG340
|
4.8
|
25.3
|
1.0
|
O1P
|
B:AHG340
|
4.9
|
36.8
|
1.0
|
N
|
B:LEU275
|
4.9
|
20.5
|
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: Mon Aug 12 04:29:04 2024
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