Magnesium in PDB 1e0c: Sulfurtransferase From Azotobacter Vinelandii

All present enzymatic activity of Sulfurtransferase From Azotobacter Vinelandii:
2.8.1.1;

The structure of Sulfurtransferase From Azotobacter Vinelandii, PDB code: 1e0c was solved by D.Bordo, D.Deriu, R.Colnaghi, A.Carpen, S.Pagani, M.Bolognesi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	40.310, 150.310, 53.390, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 23

The binding sites of Magnesium atom in the Sulfurtransferase From Azotobacter Vinelandii (pdb code 1e0c). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Sulfurtransferase From Azotobacter Vinelandii, PDB code: 1e0c:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Sulfurtransferase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Sulfurtransferase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg376 b:12.6 occ:0.50 O A:HOH2053 2.0 12.7 0.5 O A:HOH2119 2.1 10.3 0.5 O A:HOH2052 2.2 12.9 0.5 O A:HOH2121 2.2 9.9 0.5 O A:HOH2118 2.4 12.3 0.5 O A:HOH2117 2.8 9.9 0.5 O A:HOH2087 4.3 23.5 1.0 O A:HOH2201 4.3 20.9 1.0 O A:HOH2050 4.3 33.4 1.0 OE1 A:GLU70 4.4 12.7 1.0 OE2 A:GLU70 4.5 11.5 1.0 CD A:ARG66 4.7 10.4 1.0 CD A:GLU70 4.9 14.2 1.0 CB A:ALA140 5.0 15.2 1.0

Magnesium binding site 2 out of 3 in the Sulfurtransferase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Sulfurtransferase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg377 b:23.8 occ:1.00 O A:HOH2254 2.1 21.6 1.0 O A:HOH2226 2.1 25.3 1.0 O A:HOH2253 2.1 16.7 1.0 O A:HOH2228 2.2 25.1 1.0 O A:HOH2103 2.2 28.2 1.0 O A:HOH2122 2.4 27.0 1.0 OE1 A:GLU194 4.0 12.2 1.0 OE2 A:GLU194 4.1 12.5 1.0 O A:HOH2261 4.1 22.9 1.0 O A:HOH2102 4.1 16.2 1.0 O A:HOH2123 4.2 36.0 1.0 NE2 A:GLN172 4.3 22.6 1.0 O A:HOH2104 4.4 30.5 1.0 CD A:GLU194 4.4 15.1 1.0 OE1 A:GLN172 4.5 11.0 1.0 CD A:GLN172 4.9 25.4 1.0

Magnesium binding site 3 out of 3 in the Sulfurtransferase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Sulfurtransferase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg378 b:34.6 occ:1.00 O A:HOH2019 2.1 35.8 1.0 O A:HOH2020 2.1 36.7 1.0 O A:HOH2158 2.1 26.5 1.0 O A:HOH2067 2.2 38.5 1.0 O A:HOH2149 2.2 25.1 1.0 O A:HOH2058 2.4 36.3 1.0 O A:HOH2161 4.0 32.3 1.0 O A:HOH2150 4.1 12.0 1.0 O A:HOH2021 4.2 43.6 1.0 O A:HOH2153 4.3 47.7 1.0 O A:HOH2151 4.3 21.9 1.0 OE1 A:GLU90 4.3 9.9 1.0 O A:HOH2059 4.3 27.6 1.0 OD1 A:ASP89 4.4 16.0 1.0 O A:HOH2157 4.4 26.2 1.0 CB A:GLU90 4.8 9.3 1.0

D.Bordo, D.Deriu, R.Colnaghi, A.Carpen, S.Pagani, M.Bolognesi. The Crystal Structure of A Sulfurtransferase From Azotobacter Vinelandii Highlights the Evolutionary Relationship Between the Rhodanese and Phosphatase Enzyme Families J.Mol.Biol. V. 298 691 2000.
ISSN: ISSN 0022-2836
PubMed: 10788330
DOI: 10.1006/JMBI.2000.3651