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Manganese in PDB 1fpd: 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: 1fpd 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, 166.400, 79.900, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 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 1fpd). 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: 1fpd:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 1fpd

Go back to Manganese Binding Sites List in 1fpd
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:36.5
occ:0.84
 OD1 A:ASP121 2.2 19.1 1.0
OD2 A:ASP118 2.3 32.4 1.0
OE2 A:GLU280 2.3 32.6 1.0
O1P A:AHG338 2.4 48.7 1.0
OE2 A:GLU97 2.5 34.7 1.0
O3P A:AHG338 2.9 50.2 1.0
P1 A:AHG338 3.2 52.8 1.0
HH22 A:ARG276 3.3 15.0 1.0
CG A:ASP121 3.3 20.9 1.0
CG A:ASP118 3.4 27.6 1.0
H11 A:AHG338 3.5 15.0 1.0
CD A:GLU280 3.5 30.7 1.0
CD A:GLU97 3.6 36.5 1.0
NH2 A:ARG276 3.6 47.0 1.0
H A:GLY122 3.7 15.0 1.0
OD1 A:ASP118 3.8 36.5 1.0
CB A:ASP121 3.9 20.8 1.0
OE1 A:GLU97 4.0 39.6 1.0
O1 A:AHG338 4.0 42.9 1.0
HH12 A:ARG276 4.0 15.0 1.0
CA A:ASP121 4.0 21.6 1.0
HH21 A:ARG276 4.1 15.0 1.0
MN A:MN337 4.1 56.5 0.4
CZ A:ARG276 4.1 47.8 1.0
C1 A:AHG338 4.2 31.1 1.0
NH1 A:ARG276 4.3 47.7 1.0
H2 A:AHG338 4.3 15.0 1.0
OE1 A:GLU280 4.3 30.0 1.0
OD2 A:ASP121 4.4 18.8 1.0
CG A:GLU280 4.5 25.1 1.0
N A:GLY122 4.5 25.7 1.0
O2P A:AHG338 4.6 50.4 1.0
CB A:ASP118 4.6 24.3 1.0
C2 A:AHG338 4.8 25.5 1.0
CG A:GLU97 4.8 34.0 1.0
C A:ASP121 4.9 22.9 1.0
O A:LEU120 4.9 20.2 1.0
HH11 A:ARG276 5.0 15.0 1.0

Manganese binding site 2 out of 4 in 1fpd

Go back to Manganese Binding Sites List in 1fpd
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:56.5
occ:0.43
 OD1 A:ASP118 2.4 36.5 1.0
OE1 A:GLU97 2.6 39.6 1.0
O A:LEU120 2.8 20.2 1.0
OE2 A:GLU98 3.0 39.1 1.0
H A:LEU120 3.3 15.0 1.0
CD A:GLU97 3.3 36.5 1.0
CG A:ASP118 3.5 27.6 1.0
OE2 A:GLU97 3.6 34.7 1.0
C A:LEU120 3.6 19.1 1.0
HG A:SER123 3.7 15.0 1.0
OD2 A:ASP118 3.8 32.4 1.0
N A:LEU120 4.1 18.8 1.0
MN A:MN336 4.1 36.5 0.8
CD A:GLU98 4.2 35.3 1.0
OG A:SER123 4.3 50.8 1.0
CG A:GLU97 4.4 34.0 1.0
N A:ASP121 4.4 19.1 1.0
O1P A:AHG338 4.4 48.7 1.0
CD A:PRO119 4.4 15.0 1.0
CB A:GLU97 4.4 30.8 1.0
CA A:LEU120 4.4 19.6 1.0
CA A:ASP121 4.4 21.6 1.0
CG A:PRO119 4.6 18.8 1.0
CG A:GLU98 4.7 33.0 1.0
CB A:ASP118 4.8 24.3 1.0
N A:PRO119 4.8 17.6 1.0
H A:SER123 4.8 15.0 1.0
CB A:LEU120 4.9 18.0 1.0
H A:GLY122 4.9 15.0 1.0
CA A:ASP118 4.9 20.5 1.0

Manganese binding site 3 out of 4 in 1fpd

Go back to Manganese Binding Sites List in 1fpd
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:30.4
occ:0.75
 OD1 B:ASP121 2.1 18.7 1.0
OD2 B:ASP118 2.2 28.5 1.0
OE2 B:GLU280 2.3 32.5 1.0
O1P B:AHG338 2.4 44.8 1.0
OE2 B:GLU97 2.7 40.1 1.0
OE1 B:GLU97 2.8 41.1 1.0
H1 B:HOH405 2.9 15.0 1.0
CD B:GLU97 3.1 35.6 1.0
CG B:ASP118 3.2 22.9 1.0
CG B:ASP121 3.3 23.8 1.0
P1 B:AHG338 3.4 47.1 1.0
OD1 B:ASP118 3.5 30.6 1.0
CD B:GLU280 3.5 28.4 1.0
O B:HOH405 3.5 32.2 1.0
O1 B:AHG338 3.6 40.2 1.0
HH12 B:ARG276 3.7 15.0 1.0
H B:GLY122 3.8 15.0 1.0
O3P B:AHG338 3.8 45.0 1.0
CB B:ASP121 3.8 21.4 1.0
CA B:ASP121 4.0 22.8 1.0
HH11 B:ARG276 4.0 15.0 1.0
NH1 B:ARG276 4.2 48.0 1.0
H2 B:HOH405 4.2 15.0 1.0
MN B:MN337 4.2 49.5 0.4
H2 B:HOH386 4.3 15.0 1.0
CG B:GLU280 4.3 23.0 1.0
OE1 B:GLU280 4.3 29.8 1.0
OD2 B:ASP121 4.4 20.2 1.0
HO3 B:AHG338 4.4 15.0 1.0
CB B:ASP118 4.5 16.6 1.0
CG B:GLU97 4.6 34.8 1.0
N B:GLY122 4.6 29.3 1.0
H2 B:AHG338 4.7 15.0 1.0
O2P B:AHG338 4.8 45.4 1.0
C1 B:AHG338 4.9 30.6 1.0
C B:ASP121 4.9 24.5 1.0
O B:LEU120 4.9 21.6 1.0
H3 B:AHG338 5.0 15.0 1.0
N B:ASP121 5.0 20.6 1.0

Manganese binding site 4 out of 4 in 1fpd

Go back to Manganese Binding Sites List in 1fpd
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:49.5
occ:0.38
 OD1 B:ASP118 2.4 30.6 1.0
O B:LEU120 2.6 21.6 1.0
H1 B:HOH386 2.8 15.0 1.0
OE2 B:GLU98 2.8 48.2 1.0
H B:LEU120 2.8 15.0 1.0
OE2 B:GLU97 2.9 40.1 1.0
O B:HOH386 3.0 46.3 1.0
H2 B:HOH386 3.1 15.0 1.0
C B:LEU120 3.4 20.1 1.0
CG B:ASP118 3.5 22.9 1.0
N B:LEU120 3.7 18.1 1.0
CD B:GLU97 3.8 35.6 1.0
HG B:SER123 3.9 15.0 1.0
CD B:GLU98 4.0 46.3 1.0
OD2 B:ASP118 4.1 28.5 1.0
O1P B:AHG338 4.1 44.8 1.0
CA B:LEU120 4.1 21.4 1.0
CG B:PRO119 4.1 15.6 1.0
CD B:PRO119 4.2 14.9 1.0
CG B:GLU97 4.2 34.8 1.0
N B:ASP121 4.2 20.6 1.0
MN B:MN336 4.2 30.4 0.8
CA B:ASP121 4.4 22.8 1.0
CB B:GLU97 4.5 30.9 1.0
OG B:SER123 4.5 48.1 1.0
N B:PRO119 4.5 14.4 1.0
CB B:LEU120 4.6 23.3 1.0
OE1 B:GLU97 4.7 41.1 1.0
CG B:GLU98 4.7 43.0 1.0
C B:ASP118 4.8 14.7 1.0
CB B:ASP118 4.8 16.6 1.0
CA B:ASP118 4.8 16.1 1.0
C B:PRO119 4.8 17.6 1.0
CB B:ASP74 4.9 39.2 1.0
OE1 B:GLU98 4.9 51.1 1.0
H B:SER123 5.0 15.0 1.0
H B:ASP121 5.0 15.0 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 10:24:29 2024

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