Sodium in PDB 1g8f: Atp Sulfurylase From S. Cerevisiae

All present enzymatic activity of Atp Sulfurylase From S. Cerevisiae:
2.7.7.4;

The structure of Atp Sulfurylase From S. Cerevisiae, PDB code: 1g8f 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)	19.68 / 1.95
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	187.094, 187.094, 115.999, 90.00, 90.00, 120.00
R / Rfree (%)	19.6 / 23.1

The structure of Atp Sulfurylase From S. Cerevisiae also contains other interesting chemical elements:

Cadmium	(Cd)	5 atoms
Magnesium	(Mg)	1 atom
Calcium	(Ca)	3 atoms

The binding sites of Sodium atom in the Atp Sulfurylase From S. Cerevisiae (pdb code 1g8f). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Atp Sulfurylase From S. Cerevisiae, PDB code: 1g8f:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Atp Sulfurylase From S. Cerevisiae


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Atp Sulfurylase From S. Cerevisiae within 5.0Å range: probe atom residue distance (Å) B Occ A:Na518 b:32.5 occ:1.00 O A:HOH1067 3.9 58.4 1.0 O A:ASP107 4.2 43.0 1.0 CB A:ASP108 4.7 49.9 1.0 O A:HOH766 4.7 60.4 1.0

Sodium binding site 2 out of 2 in the Atp Sulfurylase From S. Cerevisiae


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Atp Sulfurylase From S. Cerevisiae within 5.0Å range: probe atom residue distance (Å) B Occ A:Na522 b:42.9 occ:1.00 OD2 A:ASP309 2.5 36.5 1.0 OD1 A:ASP309 2.8 34.7 1.0 CG A:ASP309 2.9 34.8 1.0 CB A:ASP309 4.3 31.1 1.0 CA A:GLY306 4.4 37.5 1.0 N A:GLY306 4.5 38.2 1.0 NH2 A:ARG134 4.5 38.9 1.0 O A:HOH678 4.5 41.9 1.0 NH1 A:ARG134 4.9 36.5 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