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Manganese in PDB 1fpf: 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: 1fpf 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 / 2.10
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 61.100, 166.600, 80.100, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 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 1fpf). 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: 1fpf:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 1fpf

Go back to Manganese Binding Sites List in 1fpf
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:39.7
occ:1.00
 OD2 A:ASP118 2.2 34.4 1.0
OD1 A:ASP121 2.2 19.1 1.0
OE2 A:GLU280 2.3 31.9 1.0
OE2 A:GLU97 2.4 35.5 1.0
O1P A:AHG338 2.6 43.9 1.0
HH22 A:ARG276 3.2 15.0 1.0
O3P A:AHG338 3.3 47.1 1.0
CG A:ASP118 3.3 29.2 1.0
H11 A:AHG338 3.4 15.0 1.0
CG A:ASP121 3.4 20.4 1.0
CD A:GLU280 3.4 26.2 1.0
P1 A:AHG338 3.5 49.7 1.0
NH2 A:ARG276 3.6 42.4 1.0
CD A:GLU97 3.6 33.7 1.0
OD1 A:ASP118 3.7 35.4 1.0
H A:GLY122 3.8 15.0 1.0
HH21 A:ARG276 3.9 15.0 1.0
CB A:ASP121 4.0 19.1 1.0
CA A:ASP121 4.1 20.6 1.0
HH12 A:ARG276 4.1 15.0 1.0
OE1 A:GLU280 4.1 26.9 1.0
MN A:MN337 4.1 58.9 0.8
CZ A:ARG276 4.1 42.7 1.0
C1 A:AHG338 4.3 30.7 1.0
O1 A:AHG338 4.3 40.3 1.0
CG A:GLU280 4.4 23.6 1.0
NH1 A:ARG276 4.4 43.1 1.0
H2 A:AHG338 4.4 15.0 1.0
OD2 A:ASP121 4.4 21.7 1.0
OE1 A:GLU97 4.4 37.6 1.0
CG A:GLU97 4.5 31.4 1.0
CB A:ASP118 4.6 23.9 1.0
N A:GLY122 4.7 23.2 1.0
O2P A:AHG338 4.8 46.4 1.0
C2 A:AHG338 4.9 25.9 1.0
C A:ASP121 5.0 21.9 1.0
O A:LEU120 5.0 21.3 1.0
NE A:ARG276 5.0 39.4 1.0

Manganese binding site 2 out of 4 in 1fpf

Go back to Manganese Binding Sites List in 1fpf
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:58.9
occ:0.80
 OD1 A:ASP118 2.4 35.4 1.0
OE2 A:GLU98 2.8 38.3 1.0
O A:LEU120 2.8 21.3 1.0
OE1 A:GLU97 3.0 37.6 1.0
H A:LEU120 3.3 15.0 1.0
CD A:GLU97 3.3 33.7 1.0
OE2 A:GLU97 3.3 35.5 1.0
CG A:ASP118 3.5 29.2 1.0
C A:LEU120 3.6 19.8 1.0
HG A:SER123 3.8 15.0 1.0
OD2 A:ASP118 3.9 34.4 1.0
CD A:GLU98 3.9 36.0 1.0
N A:LEU120 4.1 19.1 1.0
MN A:MN336 4.1 39.7 1.0
O1P A:AHG338 4.3 43.9 1.0
CB A:GLU97 4.3 29.5 1.0
N A:ASP121 4.4 19.5 1.0
CG A:GLU97 4.4 31.4 1.0
CG A:GLU98 4.4 34.6 1.0
CA A:LEU120 4.4 20.2 1.0
OG A:SER123 4.4 45.9 1.0
CA A:ASP121 4.5 20.6 1.0
CD A:PRO119 4.5 14.5 1.0
CG A:PRO119 4.7 15.9 1.0
CB A:ASP118 4.8 23.9 1.0
CB A:LEU120 4.9 18.0 1.0
N A:PRO119 4.9 15.1 1.0
OE1 A:GLU98 4.9 35.7 1.0
CA A:ASP118 5.0 19.3 1.0
H A:SER123 5.0 15.0 1.0

Manganese binding site 3 out of 4 in 1fpf

Go back to Manganese Binding Sites List in 1fpf
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:33.7
occ:0.92
 OD1 B:ASP121 2.1 17.6 1.0
OD2 B:ASP118 2.1 27.4 1.0
OE2 B:GLU280 2.2 29.9 1.0
O1P B:AHG338 2.5 39.7 1.0
OE1 B:GLU97 2.6 39.4 1.0
OE2 B:GLU97 2.8 39.9 1.0
CD B:GLU97 3.1 34.7 1.0
O B:HOH402 3.1 51.9 1.0
H1 B:HOH402 3.1 15.0 1.0
CG B:ASP121 3.2 22.3 1.0
CG B:ASP118 3.2 23.1 1.0
CD B:GLU280 3.4 26.9 1.0
P1 B:AHG338 3.5 44.2 1.0
OD1 B:ASP118 3.5 32.4 1.0
CB B:ASP121 3.7 19.6 1.0
O1 B:AHG338 3.7 36.6 1.0
H B:GLY122 3.8 15.0 1.0
HH12 B:ARG276 3.8 15.0 1.0
H2 B:HOH402 3.8 15.0 1.0
CA B:ASP121 3.9 19.6 1.0
O3P B:AHG338 3.9 40.9 1.0
CG B:GLU280 4.2 22.6 1.0
OD2 B:ASP121 4.3 23.2 1.0
OE1 B:GLU280 4.3 27.1 1.0
NH1 B:ARG276 4.3 48.0 1.0
HO3 B:AHG338 4.4 15.0 1.0
CB B:ASP118 4.5 16.6 1.0
MN B:MN337 4.5 50.1 0.5
N B:GLY122 4.6 24.5 1.0
CG B:GLU97 4.6 32.4 1.0
HH11 B:ARG276 4.6 15.0 1.0
H2 B:AHG338 4.7 15.0 1.0
C B:ASP121 4.8 21.9 1.0
N B:ASP121 4.9 17.2 1.0
HH22 B:ARG276 4.9 15.0 1.0
H3 B:AHG338 4.9 15.0 1.0
O2P B:AHG338 4.9 39.7 1.0
C1 B:AHG338 4.9 29.2 1.0

Manganese binding site 4 out of 4 in 1fpf

Go back to Manganese Binding Sites List in 1fpf
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:50.1
occ:0.48
 OD1 B:ASP118 2.4 32.4 1.0
H B:LEU120 2.7 15.0 1.0
O B:LEU120 2.8 20.6 1.0
OE2 B:GLU98 2.9 45.3 1.0
OE2 B:GLU97 2.9 39.9 1.0
O B:HOH387 2.9 41.0 1.0
H1 B:HOH387 3.0 15.0 1.0
C B:LEU120 3.4 18.8 1.0
N B:LEU120 3.5 18.1 1.0
H2 B:HOH387 3.6 15.0 1.0
CG B:ASP118 3.6 23.1 1.0
CD B:GLU97 3.8 34.7 1.0
CD B:PRO119 3.9 13.2 1.0
CD B:GLU98 4.0 43.8 1.0
HG B:SER123 4.0 15.0 1.0
CG B:PRO119 4.0 14.2 1.0
CA B:LEU120 4.0 19.3 1.0
N B:ASP121 4.1 17.2 1.0
OD2 B:ASP118 4.2 27.4 1.0
CG B:GLU97 4.3 32.4 1.0
N B:PRO119 4.3 13.1 1.0
O1P B:AHG338 4.4 39.7 1.0
CA B:ASP121 4.4 19.6 1.0
CB B:GLU97 4.4 28.8 1.0
CG B:GLU98 4.5 39.7 1.0
MN B:MN336 4.5 33.7 0.9
OG B:SER123 4.6 40.6 1.0
CB B:LEU120 4.6 20.4 1.0
C B:ASP118 4.6 12.7 1.0
C B:PRO119 4.7 17.2 1.0
OE1 B:GLU97 4.7 39.4 1.0
CA B:ASP118 4.8 13.6 1.0
CB B:ASP118 4.8 16.6 1.0
H B:ASP121 4.9 15.0 1.0
CA B:PRO119 4.9 15.9 1.0
CB B:ASP74 4.9 36.4 1.0
OE1 B:GLU98 5.0 47.6 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 10:24:34 2024

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