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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

Go back to 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

Go back to 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

Go back to 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

Go back to 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

Go back to 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

Go back to 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: Sun Dec 13 22:42:59 2020

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