Atomistry » Manganese » PDB 1en6-1g0i » 1fpg
Atomistry »
  Manganese »
    PDB 1en6-1g0i »
      1fpg »

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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy