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

Enzymatic activity of 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;

Protein crystallography data

The structure of Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation., PDB code: 4bvs 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) 42.29 / 2.60
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 128.365, 128.365, 228.412, 90.00, 90.00, 120.00
R / Rfree (%) 17.663 / 21.572

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cyanuric Acid Hydrolase: Evolutionary Innovation By Structural Concatenation. (pdb code 4bvs). 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: 4bvs:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4bvs

Go back to Magnesium Binding Sites List in 4bvs
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:46.4
occ:1.00
O A:ALA346 2.3 40.6 1.0
O A:GLN349 2.4 47.1 1.0
O A:PRO351 2.5 40.1 1.0
OE2 A:GLU297 2.5 50.2 1.0
O A:GLY354 2.7 47.2 1.0
C A:PRO351 3.3 41.0 1.0
C A:GLN349 3.4 41.4 1.0
C A:ALA346 3.4 40.0 1.0
CD A:GLU297 3.5 47.0 1.0
O A:GLY350 3.6 44.6 1.0
CB A:ALA346 3.6 37.7 1.0
C A:GLY350 3.8 42.1 1.0
C A:GLY354 3.8 40.7 1.0
N A:GLN349 3.8 40.5 1.0
N A:ALA352 3.9 42.5 1.0
CA A:ALA352 3.9 44.6 1.0
OE1 A:GLU297 4.0 42.3 1.0
CA A:ALA346 4.1 38.9 1.0
CA A:GLN349 4.2 41.6 1.0
N A:GLY353 4.2 44.1 1.0
N A:PRO351 4.2 41.8 1.0
N A:GLY354 4.2 42.4 1.0
N A:GLY350 4.3 44.0 1.0
CA A:PRO351 4.3 42.7 1.0
C A:ALA352 4.4 42.5 1.0
CG A:GLU297 4.4 46.6 1.0
CA A:GLY350 4.4 46.1 1.0
N A:GLU347 4.5 43.6 1.0
N A:HIS348 4.5 44.1 1.0
CB A:GLN349 4.6 40.5 1.0
N A:GLY355 4.7 43.1 1.0
CA A:GLY354 4.7 39.0 1.0
CA A:GLY355 4.7 41.9 1.0
CA A:GLU347 4.7 44.3 1.0
C A:GLU347 4.9 45.0 1.0
C A:HIS348 4.9 40.5 1.0

Magnesium binding site 2 out of 2 in 4bvs

Go back to Magnesium Binding Sites List in 4bvs
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:48.0
occ:1.00
O B:ALA346 2.2 40.7 1.0
O B:GLN349 2.4 31.9 1.0
OE2 B:GLU297 2.5 44.2 1.0
O B:PRO351 2.6 44.3 1.0
O B:GLY354 2.6 36.6 1.0
C B:ALA346 3.3 38.9 1.0
CD B:GLU297 3.4 39.3 1.0
CB B:ALA346 3.4 40.2 1.0
C B:GLN349 3.4 34.7 1.0
C B:PRO351 3.5 44.1 1.0
O B:GLY350 3.7 37.5 1.0
C B:GLY354 3.7 35.8 1.0
N B:GLN349 3.8 36.9 1.0
C B:GLY350 3.9 38.8 1.0
OE1 B:GLU297 3.9 39.7 1.0
CA B:ALA346 4.0 39.5 1.0
CA B:ALA352 4.1 40.5 1.0
N B:ALA352 4.1 42.8 1.0
CA B:GLN349 4.1 35.3 1.0
N B:GLY354 4.2 36.9 1.0
N B:GLY353 4.2 43.2 1.0
CG B:GLU297 4.3 38.1 1.0
N B:PRO351 4.3 37.2 1.0
N B:GLY350 4.4 37.1 1.0
N B:GLU347 4.4 36.1 1.0
CA B:PRO351 4.5 42.8 1.0
CA B:GLY350 4.5 37.2 1.0
CB B:GLN349 4.5 37.2 1.0
C B:ALA352 4.5 43.6 1.0
N B:GLY355 4.6 32.8 1.0
N B:HIS348 4.6 36.7 1.0
CA B:GLY355 4.6 35.7 1.0
CA B:GLY354 4.6 36.6 1.0
CA B:GLU347 4.7 36.9 1.0
C B:GLU347 4.9 37.0 1.0
C B:HIS348 5.0 34.4 1.0
N B:ALA346 5.0 39.1 1.0
C B:GLY353 5.0 37.9 1.0

Reference:

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
Page generated: Mon Dec 14 09:12:45 2020

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