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Magnesium in PDB 1g8g: Atp Sulfurylase From S. Cerevisiae: the Binary Product Complex with Aps

Enzymatic activity of Atp Sulfurylase From S. Cerevisiae: the Binary Product Complex with Aps

All present enzymatic activity of Atp Sulfurylase From S. Cerevisiae: the Binary Product Complex with Aps:
2.7.7.4;

Protein crystallography data

The structure of Atp Sulfurylase From S. Cerevisiae: the Binary Product Complex with Aps, PDB code: 1g8g was solved by T.C.Ullrich, M.Blaesse, R.Huber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.85 / 2.60
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 185.922, 185.922, 223.674, 90.00, 90.00, 120.00
R / Rfree (%) 17.6 / 22.7

Other elements in 1g8g:

The structure of Atp Sulfurylase From S. Cerevisiae: the Binary Product Complex with Aps also contains other interesting chemical elements:

Cadmium (Cd) 11 atoms
Calcium (Ca) 6 atoms
Sodium (Na) 12 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Atp Sulfurylase From S. Cerevisiae: the Binary Product Complex with Aps (pdb code 1g8g). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Atp Sulfurylase From S. Cerevisiae: the Binary Product Complex with Aps, PDB code: 1g8g:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1g8g

Go back to Magnesium Binding Sites List in 1g8g
Magnesium binding site 1 out of 2 in the Atp Sulfurylase From S. Cerevisiae: the Binary Product Complex with Aps


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Atp Sulfurylase From S. Cerevisiae: the Binary Product Complex with Aps within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg521

b:37.4
occ:1.00
O A:HOH1330 2.0 42.7 1.0
ND1 A:HIS166 2.1 25.6 1.0
CE1 A:HIS166 2.4 25.6 1.0
O A:PRO164 2.4 26.2 1.0
OE2 A:GLU46 2.6 28.3 1.0
OE1 A:GLU46 2.9 29.1 1.0
CD A:GLU46 3.0 28.5 1.0
CG A:HIS166 3.3 27.3 1.0
C A:PRO164 3.4 26.0 1.0
NE2 A:HIS166 3.6 28.8 1.0
N A:PRO164 4.1 25.6 1.0
CD2 A:HIS166 4.1 26.9 1.0
CA A:PRO164 4.1 25.1 1.0
CB A:PRO164 4.1 24.5 1.0
CB A:HIS166 4.2 27.5 1.0
CD A:ARG173 4.2 34.7 1.0
CG A:GLU46 4.3 26.2 1.0
CB A:LEU163 4.4 21.4 1.0
N A:GLN165 4.4 29.1 1.0
N A:HIS166 4.5 29.6 1.0
C A:LEU163 4.5 24.3 1.0
C A:GLN165 4.5 30.5 1.0
CD A:PRO164 4.5 25.2 1.0
NE A:ARG173 4.6 39.8 1.0
O A:HOH799 4.6 38.4 1.0
O A:HOH827 4.6 38.8 1.0
CA A:GLN165 4.7 30.6 1.0
O A:LEU163 4.8 24.0 1.0
O A:GLN165 4.9 30.0 1.0
CA A:HIS166 5.0 29.6 1.0
O A:HOH696 5.0 18.1 1.0
CG A:PRO164 5.0 22.6 1.0

Magnesium binding site 2 out of 2 in 1g8g

Go back to Magnesium Binding Sites List in 1g8g
Magnesium binding site 2 out of 2 in the Atp Sulfurylase From S. Cerevisiae: the Binary Product Complex with Aps


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Atp Sulfurylase From S. Cerevisiae: the Binary Product Complex with Aps within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg539

b:40.7
occ:1.00
ND1 B:HIS166 1.9 26.9 1.0
O B:PRO164 2.2 25.1 1.0
CE1 B:HIS166 2.4 24.5 1.0
O B:HOH1287 2.7 41.4 1.0
OE2 B:GLU46 2.8 28.1 1.0
O B:HOH1028 2.9 36.8 1.0
CG B:HIS166 3.2 27.4 1.0
C B:PRO164 3.3 28.1 1.0
CD B:GLU46 3.3 26.7 1.0
OE1 B:GLU46 3.3 27.0 1.0
NE2 B:HIS166 3.6 27.1 1.0
O B:HOH785 3.8 36.8 1.0
CB B:HIS166 4.0 28.2 1.0
CD2 B:HIS166 4.0 26.8 1.0
CA B:PRO164 4.1 26.1 1.0
N B:PRO164 4.1 25.8 1.0
C B:GLN165 4.2 30.8 1.0
N B:GLN165 4.3 31.5 1.0
CB B:PRO164 4.3 25.1 1.0
N B:HIS166 4.3 30.1 1.0
C B:LEU163 4.4 26.9 1.0
CB B:LEU163 4.4 26.7 1.0
O B:GLN165 4.4 30.3 1.0
CA B:GLN165 4.5 32.9 1.0
CG B:GLU46 4.5 23.8 1.0
O B:LEU163 4.6 26.9 1.0
CD B:PRO164 4.7 25.4 1.0
CA B:HIS166 4.8 32.0 1.0

Reference:

T.C.Ullrich, M.Blaesse, R.Huber. Crystal Structure of Atp Sulfurylase From Saccharomyces Cerevisiae, A Key Enzyme in Sulfate Activation. Embo J. V. 20 316 2001.
ISSN: ISSN 0261-4189
PubMed: 11157739
DOI: 10.1093/EMBOJ/20.3.316
Page generated: Tue Aug 13 03:42:24 2024

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