Magnesium in PDB 4bvr: Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation.

All present enzymatic activity of Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation.:
3.5.2.15;

The structure of Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation., PDB code: 4bvr was solved by T.S.Peat, S.Balotra, M.Wilding, N.G.French, L.J.Briggs, S.Panjikar, N.Cowieson, J.Newman, C.Scott, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.59 / 2.58
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	129.075, 129.075, 229.660, 90.00, 90.00, 120.00
R / Rfree (%)	17.628 / 22.442

The binding sites of Magnesium atom in the Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation. (pdb code 4bvr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation., PDB code: 4bvr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1364 b:37.3 occ:1.00 O A:ALA346 2.4 33.5 1.0 O A:GLN349 2.4 47.4 1.0 O A:PRO351 2.5 39.6 1.0 O A:GLY354 2.6 49.4 1.0 OE2 A:GLU297 2.6 44.5 1.0 CD A:GLU297 3.4 41.2 1.0 C A:PRO351 3.4 41.9 1.0 C A:ALA346 3.4 34.9 1.0 C A:GLN349 3.5 45.0 1.0 CB A:ALA346 3.5 37.0 1.0 C A:GLY354 3.6 45.1 1.0 O A:GLY350 3.8 37.8 1.0 OE1 A:GLU297 3.9 40.2 1.0 C A:GLY350 4.0 40.2 1.0 N A:GLN349 4.0 37.7 1.0 CA A:ALA352 4.0 41.7 1.0 N A:ALA352 4.1 43.0 1.0 N A:GLY354 4.1 43.6 1.0 CA A:ALA346 4.1 39.0 1.0 N A:GLY353 4.1 43.2 1.0 CG A:GLU297 4.2 40.6 1.0 CA A:GLN349 4.3 40.1 1.0 N A:PRO351 4.3 40.3 1.0 N A:GLY350 4.4 48.3 1.0 C A:ALA352 4.5 43.5 1.0 CA A:PRO351 4.5 42.2 1.0 N A:GLU347 4.5 34.4 1.0 CA A:GLY354 4.5 43.0 1.0 N A:GLY355 4.5 44.8 1.0 CA A:GLY350 4.5 41.6 1.0 CA A:GLY355 4.6 44.6 1.0 CB A:GLN349 4.6 40.2 1.0 N A:HIS348 4.7 39.7 1.0 CA A:GLU347 4.8 39.4 1.0 C A:GLY353 4.9 44.3 1.0 C A:GLU347 5.0 42.5 1.0

Magnesium binding site 2 out of 2 in the Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1364 b:43.3 occ:1.00 O B:ALA346 2.3 30.1 1.0 O B:GLN349 2.3 32.6 1.0 O B:PRO351 2.5 45.8 1.0 OE2 B:GLU297 2.6 41.4 1.0 O B:GLY354 2.7 41.4 1.0 C B:GLN349 3.4 33.9 1.0 C B:ALA346 3.4 34.0 1.0 C B:PRO351 3.4 42.1 1.0 CD B:GLU297 3.4 41.5 1.0 CB B:ALA346 3.6 33.9 1.0 O B:GLY350 3.7 39.9 1.0 C B:GLY354 3.8 37.6 1.0 N B:GLN349 3.8 32.4 1.0 C B:GLY350 3.9 39.7 1.0 OE1 B:GLU297 3.9 44.4 1.0 N B:ALA352 4.0 41.1 1.0 CA B:ALA352 4.0 41.0 1.0 CA B:ALA346 4.1 32.7 1.0 CA B:GLN349 4.1 33.1 1.0 N B:GLY354 4.2 38.2 1.0 N B:GLY353 4.2 39.9 1.0 N B:PRO351 4.3 38.2 1.0 N B:GLY350 4.3 36.9 1.0 CG B:GLU297 4.4 39.5 1.0 N B:GLU347 4.4 33.7 1.0 CA B:PRO351 4.4 42.1 1.0 CA B:GLY350 4.5 37.9 1.0 C B:ALA352 4.5 40.7 1.0 CB B:GLN349 4.5 35.8 1.0 N B:HIS348 4.5 31.3 1.0 N B:GLY355 4.6 37.2 1.0 CA B:GLY354 4.6 37.4 1.0 CA B:GLY355 4.6 38.6 1.0 CA B:GLU347 4.7 31.8 1.0 C B:GLU347 4.9 32.4 1.0 C B:HIS348 4.9 32.4 1.0

T.S.Peat, S.Balotra, M.Wilding, N.G.French, L.J.Briggs, S.Panjikar, N.Cowieson, J.Newman, C.Scott. Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation. Mol.Microbiol. V. 88 1149 2013.
ISSN: ISSN 0950-382X
PubMed: 23651355
DOI: 10.1111/MMI.12249