Magnesium in PDB 1g8h: Atp Sulfurylase From S. Cerevisiae: the Ternary Product Complex with Aps and Ppi

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

The structure of Atp Sulfurylase From S. Cerevisiae: the Ternary Product Complex with Aps and Ppi, PDB code: 1g8h 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)	24.87 / 2.80
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	186.011, 186.011, 223.812, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / 24.5

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

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

The binding sites of Magnesium atom in the Atp Sulfurylase From S. Cerevisiae: the Ternary Product Complex with Aps and Ppi (pdb code 1g8h). 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 Ternary Product Complex with Aps and Ppi, PDB code: 1g8h:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Atp Sulfurylase From S. Cerevisiae: the Ternary Product Complex with Aps and Ppi


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 Ternary Product Complex with Aps and Ppi within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg521 b:22.3 occ:1.00 O A:PRO164 2.7 28.3 1.0 ND1 A:HIS166 2.7 20.6 1.0 OE1 A:GLU46 3.0 26.3 1.0 OE2 A:GLU46 3.3 28.9 1.0 CE1 A:HIS166 3.3 19.6 1.0 CD A:GLU46 3.4 27.0 1.0 CG A:HIS166 3.8 21.6 1.0 C A:PRO164 3.9 28.3 1.0 CB A:LEU163 4.1 21.4 1.0 O A:HOH717 4.2 11.2 1.0 CB A:HIS166 4.3 24.5 1.0 N A:PRO164 4.5 26.4 1.0 NE2 A:HIS166 4.6 21.4 1.0 C A:LEU163 4.6 25.4 1.0 N A:HIS166 4.6 28.0 1.0 CD1 A:LEU163 4.7 19.3 1.0 CA A:PRO164 4.7 27.1 1.0 CG A:GLU46 4.8 26.3 1.0 O A:HOH656 4.8 13.1 1.0 CD2 A:HIS166 4.8 20.7 1.0 O A:LEU163 4.8 26.3 1.0 N A:GLN165 4.8 30.3 1.0 C A:GLN165 4.8 29.8 1.0 CA A:GLN165 5.0 30.8 1.0

Magnesium binding site 2 out of 2 in the Atp Sulfurylase From S. Cerevisiae: the Ternary Product Complex with Aps and Ppi


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 Ternary Product Complex with Aps and Ppi within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg539 b:70.4 occ:1.00 O B:PRO164 1.9 28.0 1.0 ND1 B:HIS166 2.4 24.7 1.0 CE1 B:HIS166 3.0 25.5 1.0 OE2 B:GLU46 3.1 26.1 1.0 C B:PRO164 3.2 28.9 1.0 OE1 B:GLU46 3.4 24.2 1.0 CD B:GLU46 3.5 23.9 1.0 CG B:HIS166 3.6 24.4 1.0 N B:PRO164 4.0 27.4 1.0 CA B:PRO164 4.0 27.6 1.0 N B:GLN165 4.1 29.8 1.0 CB B:LEU163 4.1 20.8 1.0 CB B:HIS166 4.1 24.6 1.0 C B:LEU163 4.2 26.7 1.0 N B:HIS166 4.2 26.4 1.0 NE2 B:HIS166 4.2 26.6 1.0 C B:GLN165 4.2 28.3 1.0 CA B:GLN165 4.3 30.6 1.0 O B:LEU163 4.3 28.6 1.0 CB B:PRO164 4.4 27.7 1.0 CD2 B:HIS166 4.5 24.4 1.0 CD B:PRO164 4.6 28.1 1.0 O B:GLN165 4.8 28.3 1.0 CA B:HIS166 4.8 27.2 1.0 CG B:GLU46 4.8 24.1 1.0 CA B:LEU163 4.8 24.4 1.0

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