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Magnesium in PDB 4bvq: 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: 4bvq 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) 43.75 / 1.90
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 130.659, 130.659, 236.947, 90.00, 90.00, 120.00
R / Rfree (%) 16.979 / 18.929

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 2 in 4bvq

Go back to Magnesium Binding Sites List in 4bvq
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:Mg1365

b:30.8
occ:1.00
O A:GLN349 2.4 28.5 1.0
O A:PRO351 2.4 31.9 1.0
O A:GLY354 2.4 24.8 1.0
O A:ALA346 2.4 25.9 1.0
OE2 A:GLU297 2.5 28.4 1.0
CB A:ALA346 3.3 24.6 1.0
CD A:GLU297 3.4 28.4 1.0
C A:PRO351 3.4 32.9 1.0
C A:GLY354 3.4 25.2 1.0
C A:GLN349 3.5 29.0 1.0
C A:ALA346 3.5 25.3 1.0
O A:GLY350 3.8 31.1 1.0
N A:GLY354 3.9 27.0 1.0
C A:GLY350 3.9 30.2 1.0
CA A:ALA346 4.0 24.7 1.0
OE1 A:GLU297 4.0 26.1 1.0
N A:GLN349 4.0 28.7 1.0
N A:GLY353 4.1 29.8 1.0
CA A:ALA352 4.1 33.6 1.0
N A:ALA352 4.1 32.1 1.0
O A:HOH2091 4.2 35.9 1.0
N A:PRO351 4.2 31.2 1.0
CA A:GLN349 4.3 29.1 1.0
CG A:GLU297 4.3 26.7 1.0
CA A:GLY354 4.3 25.7 1.0
N A:GLY355 4.3 25.1 1.0
N A:GLY350 4.4 28.1 1.0
C A:ALA352 4.4 32.0 1.0
CA A:GLY355 4.4 25.4 1.0
CA A:PRO351 4.4 33.0 1.0
CA A:GLY350 4.5 27.6 1.0
N A:GLU347 4.6 26.4 1.0
CB A:GLN349 4.6 28.6 1.0
C A:GLY353 4.7 27.2 1.0
N A:HIS348 4.8 28.6 1.0
CA A:GLY353 4.9 28.1 1.0
CA A:GLU347 5.0 27.5 1.0

Magnesium binding site 2 out of 2 in 4bvq

Go back to Magnesium Binding Sites List in 4bvq
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:Mg1365

b:20.6
occ:1.00
O B:GLN349 2.3 18.7 1.0
O B:GLY354 2.4 20.3 1.0
O B:ALA346 2.4 18.0 1.0
O B:PRO351 2.4 24.9 1.0
O B:HOH2150 2.4 32.9 1.0
OE2 B:GLU297 2.6 22.1 1.0
CB B:ALA346 3.3 19.5 1.0
CD B:GLU297 3.4 23.3 1.0
C B:GLN349 3.4 19.8 1.0
C B:PRO351 3.4 26.1 1.0
C B:ALA346 3.4 18.0 1.0
C B:GLY354 3.5 19.5 1.0
O B:GLY350 3.8 23.3 1.0
C B:GLY350 3.9 22.7 1.0
N B:GLY354 3.9 19.8 1.0
CA B:ALA346 4.0 18.6 1.0
N B:GLN349 4.0 19.1 1.0
OE1 B:GLU297 4.0 23.9 1.0
CA B:ALA352 4.1 26.3 1.0
N B:ALA352 4.1 26.2 1.0
N B:GLY353 4.1 22.6 1.0
O B:HOH2125 4.2 31.8 1.0
CA B:GLN349 4.2 19.8 1.0
N B:PRO351 4.2 25.4 1.0
CG B:GLU297 4.3 22.4 1.0
CA B:GLY354 4.3 20.1 1.0
N B:GLY355 4.3 21.6 1.0
N B:GLY350 4.4 20.5 1.0
CA B:GLY355 4.4 21.3 1.0
CA B:PRO351 4.4 27.2 1.0
CA B:GLY350 4.5 21.6 1.0
C B:ALA352 4.5 24.6 1.0
CB B:GLN349 4.5 19.1 1.0
N B:GLU347 4.6 18.7 1.0
C B:GLY353 4.8 20.9 1.0
N B:HIS348 4.8 19.7 1.0
O B:HOH2152 4.9 36.5 1.0
CA B:GLU347 5.0 19.9 1.0
N B:ALA346 5.0 18.6 1.0
CA B:GLY353 5.0 21.1 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: Thu Aug 15 16:34:02 2024

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