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Manganese in PDB 1fpe: 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: 1fpe 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 / 2.20
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 61.000, 166.500, 79.900, 90.00, 90.00, 90.00
R / Rfree (%) 18 / 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 1fpe). 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: 1fpe:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 1fpe

Go back to Manganese Binding Sites List in 1fpe
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:30.2
occ:1.00
 OD1 A:ASP121 2.1 18.3 1.0
OE2 A:GLU280 2.1 32.6 1.0
OD2 A:ASP118 2.2 32.8 1.0
O1P A:AHG338 2.3 45.8 1.0
OE2 A:GLU97 2.5 38.2 1.0
P1 A:AHG338 3.0 54.3 1.0
O3P A:AHG338 3.0 51.4 1.0
CD A:GLU280 3.2 30.0 1.0
CG A:ASP121 3.2 22.3 1.0
CG A:ASP118 3.2 28.1 1.0
O1 A:AHG338 3.3 46.7 1.0
HH22 A:ARG276 3.3 15.0 1.0
OD1 A:ASP118 3.7 37.2 1.0
CD A:GLU97 3.7 39.2 1.0
NH2 A:ARG276 3.7 47.7 1.0
CB A:ASP121 3.8 22.2 1.0
OE1 A:GLU280 3.9 29.9 1.0
HH12 A:ARG276 3.9 15.0 1.0
CG A:GLU280 4.0 24.7 1.0
CA A:ASP121 4.1 21.9 1.0
H A:GLY122 4.1 15.0 1.0
MN A:MN337 4.1 55.7 0.8
HH21 A:ARG276 4.1 15.0 1.0
CZ A:ARG276 4.2 48.4 1.0
OD2 A:ASP121 4.2 25.1 1.0
NH1 A:ARG276 4.3 48.5 1.0
CB A:ASP118 4.4 24.1 1.0
O2P A:AHG338 4.5 53.2 1.0
CG A:GLU97 4.5 37.6 1.0
OE1 A:GLU97 4.6 44.8 1.0
C1 A:AHG338 4.7 32.8 1.0
H2 A:AHG338 4.7 15.0 1.0
N A:GLY122 4.9 25.4 1.0
H3 A:AHG338 4.9 15.0 1.0
HH11 A:ARG276 5.0 15.0 1.0

Manganese binding site 2 out of 4 in 1fpe

Go back to Manganese Binding Sites List in 1fpe
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:55.7
occ:0.85
 OD1 A:ASP118 2.4 37.2 1.0
O A:LEU120 2.8 22.0 1.0
OE2 A:GLU98 2.9 38.7 1.0
OE2 A:GLU97 3.1 38.2 1.0
OE1 A:GLU97 3.1 44.8 1.0
CD A:GLU97 3.2 39.2 1.0
H A:LEU120 3.2 15.0 1.0
O1P A:AHG338 3.4 45.8 1.0
CG A:ASP118 3.5 28.1 1.0
C A:LEU120 3.6 19.8 1.0
OD2 A:ASP118 3.8 32.8 1.0
HG A:SER123 4.0 15.0 1.0
CD A:GLU98 4.1 35.4 1.0
MN A:MN336 4.1 30.2 1.0
N A:LEU120 4.1 18.6 1.0
N A:ASP121 4.3 20.5 1.0
CA A:ASP121 4.3 21.9 1.0
CB A:GLU97 4.4 34.1 1.0
CG A:GLU97 4.4 37.6 1.0
CA A:LEU120 4.4 18.8 1.0
CD A:PRO119 4.5 12.5 1.0
CG A:GLU98 4.6 34.6 1.0
CG A:PRO119 4.7 16.3 1.0
OG A:SER123 4.7 44.4 1.0
CB A:ASP118 4.8 24.1 1.0
H A:SER123 4.8 15.0 1.0
P1 A:AHG338 4.8 54.3 1.0
N A:PRO119 4.9 15.2 1.0
H A:GLY122 4.9 15.0 1.0
CB A:LEU120 4.9 17.0 1.0
CA A:ASP118 5.0 19.9 1.0

Manganese binding site 3 out of 4 in 1fpe

Go back to Manganese Binding Sites List in 1fpe
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:29.7
occ:0.92
 OD2 B:ASP118 2.1 27.2 1.0
OE2 B:GLU280 2.2 29.0 1.0
OD1 B:ASP121 2.2 21.7 1.0
O1P B:AHG338 2.4 44.6 1.0
OE2 B:GLU97 2.8 43.2 1.0
OE1 B:GLU97 2.8 40.4 1.0
CG B:ASP118 3.1 21.8 1.0
CD B:GLU97 3.2 39.0 1.0
CG B:ASP121 3.2 26.4 1.0
CD B:GLU280 3.3 24.5 1.0
OD1 B:ASP118 3.4 32.9 1.0
P1 B:AHG338 3.5 54.5 1.0
HH12 B:ARG276 3.6 15.0 1.0
O1 B:AHG338 3.6 47.0 1.0
CB B:ASP121 3.6 23.2 1.0
H2 B:HOH372 3.8 15.0 1.0
O B:HOH399 3.8 32.8 1.0
H1 B:HOH399 3.8 15.0 1.0
H B:GLY122 3.9 15.0 1.0
CA B:ASP121 3.9 23.1 1.0
O3P B:AHG338 4.0 52.9 1.0
CG B:GLU280 4.1 20.7 1.0
O B:HOH372 4.1 57.6 1.0
OE1 B:GLU280 4.2 25.6 1.0
HH11 B:ARG276 4.3 15.0 1.0
NH1 B:ARG276 4.3 52.2 1.0
OD2 B:ASP121 4.4 24.1 1.0
CB B:ASP118 4.4 18.0 1.0
H2 B:HOH399 4.4 15.0 1.0
HO3 B:AHG338 4.4 15.0 1.0
MN B:MN337 4.5 50.1 0.6
H2 B:AHG338 4.6 15.0 1.0
CG B:GLU97 4.6 35.5 1.0
N B:GLY122 4.7 27.1 1.0
O2P B:AHG338 4.8 51.6 1.0
H3 B:AHG338 4.9 15.0 1.0
C B:ASP121 4.9 24.8 1.0
N B:ASP121 4.9 20.5 1.0
C1 B:AHG338 5.0 37.5 1.0

Manganese binding site 4 out of 4 in 1fpe

Go back to Manganese Binding Sites List in 1fpe
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:0.63
 OD1 B:ASP118 2.3 32.9 1.0
O B:HOH372 2.4 57.6 1.0
H1 B:HOH372 2.4 15.0 1.0
H2 B:HOH372 2.5 15.0 1.0
H B:LEU120 2.6 15.0 1.0
OE2 B:GLU98 2.7 45.4 1.0
OE2 B:GLU97 2.9 43.2 1.0
O B:LEU120 2.9 22.8 1.0
C B:LEU120 3.5 21.3 1.0
N B:LEU120 3.5 19.6 1.0
CG B:ASP118 3.5 21.8 1.0
CD B:GLU98 3.7 44.6 1.0
CD B:GLU97 3.7 39.0 1.0
CD B:PRO119 3.8 17.2 1.0
CG B:PRO119 3.9 16.3 1.0
CG B:GLU97 4.0 35.5 1.0
HG B:SER123 4.1 15.0 1.0
CA B:LEU120 4.1 21.3 1.0
O B:HOH389 4.1 48.1 1.0
CB B:GLU97 4.1 32.8 1.0
N B:PRO119 4.2 15.5 1.0
OD2 B:ASP118 4.2 27.2 1.0
H1 B:HOH389 4.2 15.0 1.0
N B:ASP121 4.2 20.5 1.0
O1P B:AHG338 4.4 44.6 1.0
CG B:GLU98 4.4 43.0 1.0
C B:ASP118 4.5 16.4 1.0
MN B:MN336 4.5 29.7 0.9
CA B:ASP121 4.5 23.1 1.0
OE1 B:GLU98 4.5 48.8 1.0
CA B:ASP118 4.5 16.1 1.0
H2 B:HOH389 4.6 15.0 1.0
C B:PRO119 4.6 20.1 1.0
CB B:ASP118 4.6 18.0 1.0
OE1 B:GLU97 4.6 40.4 1.0
OG B:SER123 4.7 37.3 1.0
CB B:LEU120 4.7 22.9 1.0
CA B:PRO119 4.8 18.6 1.0
H B:ASP121 4.9 15.0 1.0
CB B:PRO119 5.0 15.2 1.0
H B:GLU98 5.0 15.0 1.0
CB B:ASP74 5.0 39.5 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 10:24:32 2024

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