Atomistry » Magnesium » PDB 1q3b-1qc1 » 1q9d
Atomistry »
  Magnesium »
    PDB 1q3b-1qc1 »
      1q9d »

Magnesium in PDB 1q9d: Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State)

Enzymatic activity of Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State)

All present enzymatic activity of Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State):
3.1.3.11;

Protein crystallography data

The structure of Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State), PDB code: 1q9d was solved by R.B.Honzatko, J.Y.Choe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.35
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 58.860, 166.250, 80.270, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 24.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State) (pdb code 1q9d). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State), PDB code: 1q9d:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1q9d

Go back to Magnesium Binding Sites List in 1q9d
Magnesium binding site 1 out of 4 in the Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg404

b:18.2
occ:1.00
OE1 A:GLU280 2.1 21.1 1.0
OD2 A:ASP121 2.1 28.2 1.0
O1 A:PO4403 2.1 43.6 1.0
OD2 A:ASP118 2.2 31.4 1.0
CG A:ASP121 3.0 27.2 1.0
CD A:GLU280 3.1 20.6 1.0
CG A:ASP118 3.2 24.3 1.0
CB A:ASP121 3.2 24.2 1.0
P A:PO4403 3.2 45.9 1.0
O3 A:PO4403 3.5 42.9 1.0
O4 A:PO4403 3.6 44.6 1.0
CG A:GLU280 3.6 19.9 1.0
CA A:ASP121 3.6 21.2 1.0
OD1 A:ASP118 3.7 22.1 1.0
OE2 A:GLU97 3.9 35.8 1.0
C1 A:F6P401 4.0 23.6 1.0
OE2 A:GLU280 4.1 20.7 1.0
OD1 A:ASP121 4.2 26.1 1.0
CB A:ASP118 4.3 23.4 1.0
O3 A:F6P401 4.3 19.6 1.0
MG A:MG405 4.5 28.6 1.0
O2 A:PO4403 4.5 44.6 1.0
CD A:GLU97 4.5 31.9 1.0
N A:GLY122 4.5 19.8 1.0
OE1 A:GLU97 4.5 32.3 1.0
O A:HOH634 4.5 37.9 1.0
O1 A:F6P401 4.6 22.9 1.0
C A:ASP121 4.6 20.7 1.0
N A:ASP121 4.6 21.3 1.0
CD1 A:ILE135 4.7 21.1 1.0
O A:LEU120 4.7 21.3 1.0
C2 A:F6P401 4.7 23.9 1.0
O2 A:F6P401 4.7 22.2 1.0
C3 A:F6P401 4.9 23.9 1.0

Magnesium binding site 2 out of 4 in 1q9d

Go back to Magnesium Binding Sites List in 1q9d
Magnesium binding site 2 out of 4 in the Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg405

b:28.6
occ:1.00
O4 A:PO4403 2.1 44.6 1.0
OD1 A:ASP118 2.2 22.1 1.0
OE2 A:GLU97 2.3 35.8 1.0
O A:LEU120 2.4 21.3 1.0
OE1 A:GLU98 2.8 36.0 1.0
CG A:ASP118 3.2 24.3 1.0
C A:LEU120 3.3 20.2 1.0
CD A:GLU97 3.5 31.9 1.0
P A:PO4403 3.5 45.9 1.0
OD2 A:ASP118 3.6 31.4 1.0
N A:LEU120 3.9 18.4 1.0
O1 A:PO4403 3.9 43.6 1.0
CD A:GLU98 4.1 33.3 1.0
CA A:LEU120 4.1 20.0 1.0
N A:ASP121 4.2 21.3 1.0
O2 A:PO4403 4.2 44.6 1.0
CB A:GLU97 4.2 27.2 1.0
CG A:GLU97 4.3 29.7 1.0
OE1 A:GLU97 4.3 32.3 1.0
CA A:ASP121 4.4 21.2 1.0
MG A:MG404 4.5 18.2 1.0
O3 A:PO4403 4.5 42.9 1.0
CB A:ASP118 4.5 23.4 1.0
CD A:PRO119 4.6 18.2 1.0
OG A:SER123 4.6 34.7 1.0
CB A:LEU120 4.6 21.5 1.0
CG A:PRO119 4.6 16.7 1.0
N A:PRO119 4.7 20.2 1.0
CA A:ASP118 4.8 22.3 1.0
C A:ASP118 4.8 21.5 1.0
OE2 A:GLU98 4.9 34.5 1.0

Magnesium binding site 3 out of 4 in 1q9d

Go back to Magnesium Binding Sites List in 1q9d
Magnesium binding site 3 out of 4 in the Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg414

b:9.7
occ:1.00
O4 B:PO4413 2.0 46.3 1.0
OD2 B:ASP118 2.1 22.9 1.0
OD2 B:ASP121 2.2 18.5 1.0
OE1 B:GLU280 2.3 17.5 1.0
P B:PO4413 2.9 48.1 1.0
CG B:ASP121 3.0 21.0 1.0
O2 B:PO4413 3.1 46.4 1.0
CB B:ASP121 3.2 21.2 1.0
CD B:GLU280 3.2 15.9 1.0
CG B:ASP118 3.3 19.7 1.0
O1 B:PO4413 3.3 45.4 1.0
CA B:ASP121 3.5 21.1 1.0
CG B:GLU280 3.6 16.8 1.0
C1 B:F6P411 3.6 29.9 1.0
OE2 B:GLU97 3.7 31.1 1.0
OD1 B:ASP118 3.8 21.0 1.0
OD1 B:ASP121 4.2 21.1 1.0
N B:GLY122 4.2 22.6 1.0
O3 B:PO4413 4.2 46.0 1.0
O1 B:F6P411 4.3 33.3 1.0
OE2 B:GLU280 4.3 16.0 1.0
C B:ASP121 4.4 21.6 1.0
CB B:ASP118 4.5 17.3 1.0
N B:ASP121 4.5 19.8 1.0
O3 B:F6P411 4.5 27.4 1.0
C2 B:F6P411 4.7 27.9 1.0
O B:LEU120 4.7 22.9 1.0
C3 B:F6P411 4.8 27.4 1.0
CD B:GLU97 4.9 27.5 1.0
C B:LEU120 5.0 21.1 1.0
O2 B:F6P411 5.0 25.8 1.0

Magnesium binding site 4 out of 4 in 1q9d

Go back to Magnesium Binding Sites List in 1q9d
Magnesium binding site 4 out of 4 in the Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Fructose-1,6-Bisphosphatase Complexed with A New Allosteric Site Inhibitor (I-State) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg415

b:31.6
occ:1.00
OD1 B:ASP118 2.4 21.0 1.0
O1 B:PO4413 2.4 45.4 1.0
OE1 B:GLU98 2.4 33.8 1.0
O B:LEU120 2.6 22.9 1.0
O B:HOH752 3.0 56.7 1.0
O B:HOH780 3.4 43.0 1.0
C B:LEU120 3.5 21.1 1.0
CG B:ASP118 3.6 19.7 1.0
CD B:GLU98 3.6 31.0 1.0
N B:LEU120 3.7 21.2 1.0
OE1 B:GLU97 3.7 27.9 1.0
CD B:GLU97 3.9 27.5 1.0
P B:PO4413 3.9 48.1 1.0
CG B:PRO119 4.0 20.4 1.0
OE2 B:GLU97 4.0 31.1 1.0
CA B:LEU120 4.1 21.4 1.0
CD B:PRO119 4.2 19.8 1.0
OD2 B:ASP118 4.3 22.9 1.0
CB B:GLU97 4.3 22.6 1.0
N B:PRO119 4.4 19.6 1.0
CG B:GLU98 4.4 28.7 1.0
N B:ASP121 4.5 19.8 1.0
C B:ASP118 4.5 18.0 1.0
O4 B:PO4413 4.5 46.3 1.0
OE2 B:GLU98 4.5 30.6 1.0
O3 B:PO4413 4.6 46.0 1.0
CA B:ASP118 4.6 17.6 1.0
CG B:GLU97 4.6 28.7 1.0
CB B:LEU120 4.7 20.3 1.0
O2 B:PO4413 4.7 46.4 1.0
CB B:ASP118 4.7 17.3 1.0
C B:PRO119 4.8 20.8 1.0
CA B:ASP121 4.9 21.1 1.0
CA B:PRO119 4.9 19.7 1.0
CB B:PRO119 5.0 20.2 1.0

Reference:

J.Y.Choe, S.W.Nelson, K.L.Arienti, F.U.Axe, T.L.Collins, T.K.Jones, R.D.Kimmich, M.J.Newman, K.Norvell, W.C.Ripka, S.J.Romano, K.M.Short, D.H.Slee, H.J.Fromm, R.B.Honzatko. Inhibition of Fructose-1,6-Bisphosphatase By A New Class of Allosteric Effectors J.Biol.Chem. V. 278 51176 2003.
ISSN: ISSN 0021-9258
PubMed: 14530289
DOI: 10.1074/JBC.M308396200
Page generated: Tue Aug 13 11:09:29 2024

Last articles

Sr in 1SFC
Sr in 1OQ7
Sr in 1U3E
Sr in 1VC0
Sr in 1F1T
Sr in 1J8G
Sr in 1NVY
Sr in 1TJM
Sr in 1NUV
Sr in 1M6G
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy