Magnesium in PDB 5t13: Structure of the Cyanuric Acid Hydrolase Trzd Reveals Product Exit Channel

All present enzymatic activity of Structure of the Cyanuric Acid Hydrolase Trzd Reveals Product Exit Channel:
3.5.2.15;

The structure of Structure of the Cyanuric Acid Hydrolase Trzd Reveals Product Exit Channel, PDB code: 5t13 was solved by A.K.Bera, L.P.Wackett, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.45 / 2.19
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	67.591, 90.686, 120.075, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 20

The binding sites of Magnesium atom in the Structure of the Cyanuric Acid Hydrolase Trzd Reveals Product Exit Channel (pdb code 5t13). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of the Cyanuric Acid Hydrolase Trzd Reveals Product Exit Channel, PDB code: 5t13:

Magnesium binding site 1 out of 1 in the Structure of the Cyanuric Acid Hydrolase Trzd Reveals Product Exit Channel


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Cyanuric Acid Hydrolase Trzd Reveals Product Exit Channel within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:22.9 occ:1.00 O A:SER352 2.6 25.8 1.0 O A:PRO357 2.6 26.9 1.0 O A:GLN355 2.6 25.0 1.0 O A:HOH634 2.7 27.0 1.0 OG A:SER352 2.9 38.2 1.0 OE2 A:GLU303 2.9 36.8 1.0 HG A:SER352 2.9 45.8 1.0 O A:GLY360 2.9 27.9 1.0 HB2 A:SER352 3.2 43.4 1.0 O A:GLY356 3.3 26.7 1.0 HA A:ALA358 3.3 41.3 1.0 H A:GLY360 3.3 31.5 1.0 H A:GLN355 3.3 32.3 1.0 C A:PRO357 3.5 30.4 1.0 CB A:SER352 3.5 36.2 1.0 C A:GLN355 3.5 26.9 1.0 C A:SER352 3.6 27.0 1.0 CD A:GLU303 3.7 34.3 1.0 C A:GLY356 3.7 27.1 1.0 H A:GLY359 3.7 43.4 1.0 C A:GLY360 3.8 26.8 1.0 N A:GLN355 4.0 26.9 1.0 CA A:ALA358 4.0 34.5 1.0 N A:GLY360 4.0 26.2 1.0 O A:HOH597 4.1 33.2 1.0 N A:ALA358 4.1 30.2 1.0 HA3 A:GLY356 4.1 31.4 1.0 OE1 A:GLU303 4.1 31.6 1.0 N A:GLY359 4.1 36.1 1.0 CA A:SER352 4.2 30.9 1.0 HA2 A:GLY361 4.2 33.7 1.0 N A:PRO357 4.2 24.7 1.0 HG2 A:GLU303 4.3 36.1 1.0 CA A:GLY356 4.3 26.2 1.0 N A:GLY356 4.3 27.4 1.0 HB2 A:GLN355 4.3 32.7 1.0 O A:HOH569 4.3 27.4 1.0 CA A:GLN355 4.3 26.3 1.0 HB3 A:SER352 4.4 43.4 1.0 C A:ALA358 4.4 33.2 1.0 H A:HIS354 4.4 31.5 1.0 CA A:PRO357 4.4 26.3 1.0 CA A:GLY360 4.5 28.0 1.0 HA A:GLU353 4.5 30.8 1.0 CG A:GLU303 4.6 30.1 1.0 N A:GLU353 4.6 26.8 1.0 N A:GLY361 4.6 27.4 1.0 N A:HIS354 4.7 26.2 1.0 CA A:GLY361 4.8 28.1 1.0 HA A:PRO357 4.8 31.6 1.0 HA A:SER352 4.8 37.0 1.0 H A:ALA358 4.8 36.2 1.0 HA3 A:GLY361 4.9 33.7 1.0 HA3 A:GLY360 4.9 33.5 1.0 CB A:GLN355 4.9 27.3 1.0 H A:SER352 4.9 30.8 1.0 CA A:GLU353 4.9 25.7 1.0 C A:GLY359 5.0 28.2 1.0

A.K.Bera, K.G.Aukema, M.Elias, L.P.Wackett. Structure of the Cyanuric Acid Hydrolase Trzd Reveals Product Exit Channel. Sci Rep V. 7 45277 2017.
ISSN: ESSN 2045-2322
PubMed: 28345631
DOI: 10.1038/SREP45277