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Manganese in PDB 1fpg: Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography

Enzymatic activity of Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography

All present enzymatic activity of Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography:
3.1.3.11;

Protein crystallography data

The structure of Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography, PDB code: 1fpg was solved by V.Villeret, S.Huang, Y.Zhang, 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 (°) 61.100, 166.500, 80.000, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / n/a

Manganese Binding Sites:

The binding sites of Manganese atom in the Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography (pdb code 1fpg). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography, PDB code: 1fpg:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 1fpg

Go back to Manganese Binding Sites List in 1fpg
Manganese binding site 1 out of 4 in the Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn336

b:30.9
occ:0.98
 O1P A:AHG338 2.1 54.6 1.0
OD1 A:ASP121 2.1 18.2 1.0
OD2 A:ASP118 2.2 35.5 1.0
OE1 A:GLU280 2.3 41.4 1.0
O3P A:AHG338 2.4 55.1 1.0
OE1 A:GLU97 2.5 39.5 1.0
P1 A:AHG338 2.6 59.2 1.0
CD A:GLU280 2.9 36.2 1.0
CG A:ASP118 3.2 30.8 1.0
CG A:ASP121 3.2 24.7 1.0
O1 A:AHG338 3.3 53.1 1.0
OE2 A:GLU280 3.4 38.4 1.0
CD A:GLU97 3.6 41.6 1.0
HH22 A:ARG276 3.6 15.0 1.0
NH2 A:ARG276 3.7 54.5 1.0
OD1 A:ASP118 3.7 37.8 1.0
HH21 A:ARG276 3.8 15.0 1.0
CB A:ASP121 3.8 24.2 1.0
CG A:GLU280 3.9 32.2 1.0
O2P A:AHG338 4.0 55.0 1.0
OE2 A:GLU97 4.0 44.6 1.0
MN A:MN337 4.1 46.3 0.8
CA A:ASP121 4.2 23.9 1.0
H A:GLY122 4.2 15.0 1.0
OD2 A:ASP121 4.3 25.5 1.0
CB A:ASP118 4.3 27.1 1.0
CZ A:ARG276 4.3 53.3 1.0
C1 A:AHG338 4.4 42.9 1.0
H11 A:AHG338 4.4 15.0 1.0
H2 A:AHG338 4.4 15.0 1.0
H3 A:AHG338 4.7 15.0 1.0
HH12 A:ARG276 4.8 15.0 1.0
CG A:GLU97 4.8 39.1 1.0
C2 A:AHG338 4.8 35.5 1.0
NH1 A:ARG276 4.8 52.4 1.0
NE A:ARG276 4.9 50.7 1.0
N A:GLY122 5.0 28.8 1.0

Manganese binding site 2 out of 4 in 1fpg

Go back to Manganese Binding Sites List in 1fpg
Manganese binding site 2 out of 4 in the Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn337

b:46.3
occ:0.75
 OD1 A:ASP118 2.4 37.8 1.0
O A:LEU120 2.6 23.8 1.0
OE2 A:GLU97 2.8 44.6 1.0
OE2 A:GLU98 3.1 40.6 1.0
CD A:GLU97 3.2 41.6 1.0
OE1 A:GLU97 3.3 39.5 1.0
H A:LEU120 3.4 15.0 1.0
CG A:ASP118 3.5 30.8 1.0
C A:LEU120 3.6 22.8 1.0
HG A:SER123 3.8 15.0 1.0
OD2 A:ASP118 3.8 35.5 1.0
O3P A:AHG338 3.8 55.1 1.0
O1P A:AHG338 3.9 54.6 1.0
O2P A:AHG338 4.1 55.0 1.0
MN A:MN336 4.1 30.9 1.0
P1 A:AHG338 4.1 59.2 1.0
OG A:SER123 4.2 54.1 1.0
CG A:GLU97 4.2 39.1 1.0
CD A:GLU98 4.2 36.9 1.0
N A:LEU120 4.3 22.4 1.0
CA A:ASP121 4.3 23.9 1.0
N A:ASP121 4.3 23.3 1.0
CB A:GLU97 4.3 36.0 1.0
CA A:LEU120 4.5 22.9 1.0
H A:GLY122 4.7 15.0 1.0
CD A:PRO119 4.7 15.9 1.0
CB A:ASP118 4.8 27.1 1.0
H A:SER123 4.8 15.0 1.0
CG A:GLU98 4.9 36.8 1.0
CA A:ASP118 5.0 23.3 1.0
CG A:PRO119 5.0 17.8 1.0
N A:PRO119 5.0 16.7 1.0

Manganese binding site 3 out of 4 in 1fpg

Go back to Manganese Binding Sites List in 1fpg
Manganese binding site 3 out of 4 in the Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn336

b:33.2
occ:1.00
 OD1 B:ASP121 2.1 22.0 1.0
OE2 B:GLU280 2.1 37.2 1.0
OD2 B:ASP118 2.2 35.5 1.0
O1P B:AHG338 2.4 56.5 1.0
OE2 B:GLU97 2.7 48.4 1.0
OE1 B:GLU97 2.8 47.4 1.0
H1 B:HOH403 2.8 15.0 1.0
CG B:ASP118 3.1 28.2 1.0
CD B:GLU97 3.1 42.8 1.0
CG B:ASP121 3.2 28.2 1.0
O B:HOH403 3.2 46.4 1.0
CD B:GLU280 3.3 32.2 1.0
OD1 B:ASP118 3.4 38.5 1.0
P1 B:AHG338 3.4 66.9 1.0
O1 B:AHG338 3.7 55.5 1.0
CB B:ASP121 3.7 25.9 1.0
HH12 B:ARG276 3.8 15.0 1.0
H B:GLY122 3.9 15.0 1.0
CA B:ASP121 3.9 25.4 1.0
CG B:GLU280 4.0 27.4 1.0
O3P B:AHG338 4.0 65.8 1.0
H2 B:HOH403 4.1 15.0 1.0
MN B:MN337 4.2 44.6 0.7
OE1 B:GLU280 4.2 32.7 1.0
OD2 B:ASP121 4.3 27.0 1.0
HH11 B:ARG276 4.3 15.0 1.0
CB B:ASP118 4.3 23.3 1.0
NH1 B:ARG276 4.4 53.9 1.0
HO3 B:AHG338 4.4 15.0 1.0
CG B:GLU97 4.6 40.6 1.0
H1 B:HOH387 4.7 15.0 1.0
N B:GLY122 4.7 31.2 1.0
O2P B:AHG338 4.7 64.9 1.0
H2 B:AHG338 4.7 15.0 1.0
H3 B:AHG338 4.8 15.0 1.0
C B:ASP121 4.8 28.5 1.0
N B:ASP121 4.9 23.4 1.0
O B:LEU120 4.9 23.0 1.0
C1 B:AHG338 4.9 42.3 1.0

Manganese binding site 4 out of 4 in 1fpg

Go back to Manganese Binding Sites List in 1fpg
Manganese binding site 4 out of 4 in the Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Structural Aspects of the Allosteric Inhibition of Fructose-1,6- Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2, 5-Anhydro-D-Glucitol-1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn337

b:44.6
occ:0.69
 OD1 B:ASP118 2.3 38.5 1.0
O B:LEU120 2.6 23.0 1.0
OE2 B:GLU98 2.7 51.0 1.0
OE2 B:GLU97 2.9 48.4 1.0
H B:LEU120 2.9 15.0 1.0
O B:HOH387 3.1 43.8 1.0
H1 B:HOH387 3.3 15.0 1.0
C B:LEU120 3.5 23.3 1.0
CG B:ASP118 3.5 28.2 1.0
CD B:GLU97 3.6 42.8 1.0
O1P B:AHG338 3.7 56.5 1.0
N B:LEU120 3.8 21.4 1.0
CD B:GLU98 3.9 50.0 1.0
HG B:SER123 4.0 15.0 1.0
CG B:GLU97 4.0 40.6 1.0
OD2 B:ASP118 4.1 35.5 1.0
H2 B:HOH387 4.1 15.0 1.0
MN B:MN336 4.2 33.2 1.0
CB B:GLU97 4.2 38.0 1.0
CA B:LEU120 4.2 23.6 1.0
N B:ASP121 4.2 23.4 1.0
CD B:PRO119 4.3 17.5 1.0
CA B:ASP121 4.4 25.4 1.0
CG B:PRO119 4.4 16.5 1.0
OE1 B:GLU97 4.5 47.4 1.0
N B:PRO119 4.6 18.0 1.0
OG B:SER123 4.6 50.4 1.0
CB B:ASP118 4.7 23.3 1.0
CG B:GLU98 4.7 46.8 1.0
C B:ASP118 4.7 18.7 1.0
CA B:ASP118 4.8 21.0 1.0
OE1 B:GLU98 4.8 55.2 1.0
CB B:LEU120 4.8 25.0 1.0
C B:PRO119 5.0 20.4 1.0

Reference:

V.Villeret, S.Huang, Y.Zhang, W.N.Lipscomb. Structural Aspects of the Allosteric Inhibition of Fructose-1,6-Bisphosphatase By Amp: the Binding of Both the Substrate Analogue 2,5-Anhydro-D-Glucitol 1,6-Bisphosphate and Catalytic Metal Ions Monitored By X-Ray Crystallography. Biochemistry V. 34 4307 1995.
ISSN: ISSN 0006-2960
PubMed: 7703244
DOI: 10.1021/BI00013A020
Page generated: Sat Oct 5 10:24:53 2024

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