Magnesium in PDB 4bvt: 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: 4bvt 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)	43.18 / 3.10
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	129.230, 129.230, 233.791, 90.00, 90.00, 120.00
R / Rfree (%)	16.4 / 20.9

The binding sites of Magnesium atom in the Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation (pdb code 4bvt). 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: 4bvt:
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:50.2 occ:1.00 O A:PRO351 2.3 51.0 1.0 O A:ALA346 2.3 54.0 1.0 O A:GLN349 2.4 55.3 1.0 O A:GLY354 2.7 54.2 1.0 OE2 A:GLU297 2.8 54.9 1.0 C A:PRO351 3.2 51.5 1.0 O A:GLY350 3.2 49.5 1.0 C A:ALA346 3.4 53.1 1.0 C A:GLN349 3.4 53.4 1.0 CB A:ALA346 3.4 52.7 1.0 CD A:GLU297 3.5 56.4 1.0 C A:GLY350 3.6 51.5 1.0 C A:GLY354 3.8 53.6 1.0 N A:GLN349 3.8 53.3 1.0 N A:ALA352 3.9 51.8 1.0 CA A:ALA352 3.9 53.8 1.0 CA A:ALA346 4.0 53.0 1.0 N A:PRO351 4.1 52.8 1.0 CA A:GLN349 4.1 53.1 1.0 OE1 A:GLU297 4.1 53.0 1.0 CA A:PRO351 4.2 50.8 1.0 N A:GLY350 4.3 52.8 1.0 N A:GLY354 4.3 53.8 1.0 CG A:GLU297 4.4 56.8 1.0 N A:GLY353 4.4 52.5 1.0 CA A:GLY350 4.4 52.2 1.0 N A:HIS348 4.5 57.3 1.0 N A:GLU347 4.5 55.3 1.0 C A:ALA352 4.5 52.6 1.0 CB A:GLN349 4.5 53.6 1.0 CA A:GLY354 4.6 52.8 1.0 N A:GLY355 4.6 53.9 1.0 CA A:GLY355 4.7 54.2 1.0 CA A:GLU347 4.8 59.6 1.0 C A:HIS348 4.9 52.8 1.0 C A:GLU347 4.9 59.7 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:49.8 occ:1.00 O B:ALA346 2.2 49.5 1.0 O B:PRO351 2.3 56.6 1.0 O B:GLN349 2.4 54.7 1.0 O B:GLY354 2.8 52.6 1.0 OE2 B:GLU297 2.8 58.7 1.0 O B:GLY350 3.1 52.9 1.0 C B:PRO351 3.2 55.6 1.0 C B:GLN349 3.3 56.3 1.0 C B:ALA346 3.3 49.3 1.0 CB B:ALA346 3.4 52.0 1.0 C B:GLY350 3.6 57.0 1.0 N B:GLN349 3.6 54.4 1.0 CD B:GLU297 3.6 56.1 1.0 N B:ALA352 3.9 54.0 1.0 C B:GLY354 3.9 53.9 1.0 CA B:GLN349 4.0 55.1 1.0 CA B:ALA352 4.0 53.8 1.0 CA B:ALA346 4.0 50.5 1.0 N B:PRO351 4.1 56.6 1.0 N B:GLY350 4.1 57.2 1.0 OE1 B:GLU297 4.2 60.3 1.0 CA B:PRO351 4.3 55.3 1.0 N B:HIS348 4.3 51.4 1.0 CA B:GLY350 4.3 57.4 1.0 N B:GLU347 4.4 47.7 1.0 CB B:GLN349 4.4 53.9 1.0 N B:GLY354 4.4 53.5 1.0 CG B:GLU297 4.5 53.6 1.0 N B:GLY353 4.5 55.4 1.0 C B:ALA352 4.6 54.8 1.0 C B:HIS348 4.7 53.9 1.0 CA B:GLU347 4.7 48.8 1.0 C B:GLU347 4.7 50.4 1.0 CA B:GLY355 4.7 53.1 1.0 N B:GLY355 4.8 53.4 1.0 CA B:GLY354 4.8 54.2 1.0 CA B:HIS348 4.9 52.0 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