Magnesium in PDB 4nq3: Crystal Structure of Cyanuic Acid Hydrolase From A. Caulinodans

The structure of Crystal Structure of Cyanuic Acid Hydrolase From A. Caulinodans, PDB code: 4nq3 was solved by S.Cho, K.Shi, H.Aihara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.79 / 2.70
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	237.866, 237.866, 105.313, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 19.1

The binding sites of Magnesium atom in the Crystal Structure of Cyanuic Acid Hydrolase From A. Caulinodans (pdb code 4nq3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Cyanuic Acid Hydrolase From A. Caulinodans, PDB code: 4nq3:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Cyanuic Acid Hydrolase From A. Caulinodans


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Cyanuic Acid Hydrolase From A. Caulinodans within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg409 b:38.9 occ:1.00 O A:GLN339 2.4 41.5 1.0 O A:PRO341 2.5 37.4 1.0 O A:GLY344 2.6 31.5 1.0 OE1 A:GLU287 2.6 62.5 1.0 O A:GLY336 2.7 32.3 1.0 O A:GLY340 3.0 29.3 1.0 C A:GLN339 3.2 31.0 1.0 C A:GLY340 3.3 30.1 1.0 C A:GLY344 3.4 31.0 1.0 C A:PRO341 3.5 33.0 1.0 C A:GLY336 3.6 31.1 1.0 CD A:GLU287 3.7 61.8 1.0 CA A:GLY340 3.8 35.0 1.0 N A:PRO341 3.9 32.9 1.0 N A:GLY344 3.9 27.7 1.0 N A:GLY340 3.9 31.5 1.0 CA A:GLY336 3.9 23.9 1.0 O A:HOH541 4.0 41.3 1.0 N A:GLN339 4.0 29.0 1.0 N A:GLY345 4.1 25.2 1.0 CA A:GLN339 4.1 28.6 1.0 CA A:GLY344 4.1 34.8 1.0 CA A:GLY345 4.2 23.9 1.0 CA A:PRO341 4.3 30.5 1.0 OE2 A:GLU287 4.3 66.2 1.0 N A:GLY343 4.3 36.4 1.0 N A:ASP342 4.4 33.9 1.0 CA A:ASP342 4.5 42.5 1.0 CB A:GLU287 4.6 44.0 1.0 CB A:GLN339 4.6 25.0 1.0 CG A:GLU287 4.7 52.9 1.0 C A:ASP342 4.8 45.6 1.0 CD A:PRO341 4.8 36.9 1.0 C A:GLY343 4.8 36.1 1.0 N A:GLU337 4.9 30.4 1.0 N A:GLY336 5.0 31.0 1.0 N A:HIS338 5.0 29.1 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Cyanuic Acid Hydrolase From A. Caulinodans


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Cyanuic Acid Hydrolase From A. Caulinodans within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg410 b:59.9 occ:1.00 O A:HOH604 2.3 65.6 1.0 O A:HOH530 2.7 49.2 1.0 OE1 A:GLU329 3.2 50.8 1.0 OE2 A:GLU329 3.3 48.5 1.0 CD A:GLU329 3.7 44.2 1.0 O A:ARG8 3.8 32.3 1.0 N A:ALA10 4.0 27.0 1.0 CB A:ALA10 4.2 22.1 1.0 CE B:LYS297 4.4 55.0 1.0 OE2 A:GLU278 4.6 91.6 1.0 CA A:ALA10 4.6 28.6 1.0 C A:ARG8 4.6 25.9 1.0 C A:ILE9 4.7 26.9 1.0 CA A:ILE9 4.8 18.8 1.0 NZ B:LYS297 4.9 58.4 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Cyanuic Acid Hydrolase From A. Caulinodans


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Cyanuic Acid Hydrolase From A. Caulinodans within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg406 b:55.9 occ:1.00 O B:PRO341 2.5 54.4 1.0 OE1 B:GLU287 2.5 73.7 1.0 O B:GLY336 2.6 49.4 1.0 O B:GLY344 2.7 46.3 1.0 O B:GLN339 2.7 60.0 1.0 O B:GLY340 3.0 53.4 1.0 C B:GLY340 3.3 56.5 1.0 C B:PRO341 3.4 56.7 1.0 C B:GLN339 3.5 51.0 1.0 CD B:GLU287 3.5 73.2 1.0 C B:GLY336 3.5 50.6 1.0 C B:GLY344 3.5 46.7 1.0 CA B:GLY336 3.8 48.1 1.0 CA B:GLY340 3.9 47.4 1.0 N B:PRO341 3.9 54.3 1.0 N B:GLY344 4.0 53.2 1.0 OE2 B:GLU287 4.0 78.2 1.0 N B:GLY340 4.1 47.8 1.0 N B:ASP342 4.1 56.0 1.0 N B:GLN339 4.2 48.5 1.0 CA B:ASP342 4.2 49.7 1.0 CA B:PRO341 4.2 51.1 1.0 N B:GLY343 4.3 56.8 1.0 CA B:GLY344 4.3 45.9 1.0 N B:GLY345 4.3 46.6 1.0 CA B:GLN339 4.4 51.7 1.0 CA B:GLY345 4.5 47.1 1.0 CB B:GLU287 4.5 59.2 1.0 CG B:GLU287 4.6 67.0 1.0 C B:ASP342 4.6 54.7 1.0 N B:GLU337 4.7 48.5 1.0 N B:GLY336 4.8 51.7 1.0 CB B:GLN339 4.9 48.8 1.0 N B:HIS338 4.9 54.3 1.0 CD B:PRO341 4.9 46.8 1.0 C B:GLY343 4.9 51.0 1.0

S.Cho, K.Shi, J.L.Seffernick, A.G.Dodge, L.P.Wackett, H.Aihara. Cyanuric Acid Hydrolase From Azorhizobium Caulinodans Ors 571: Crystal Structure and Insights Into A New Class of Ser-Lys Dyad Proteins. Plos One V. 9 99349 2014.
ISSN: ESSN 1932-6203
PubMed: 24915109
DOI: 10.1371/JOURNAL.PONE.0099349