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Magnesium in PDB 1lnt: Crystal Structure of the Highly Conserved Rna Internal Loop of Srp

Protein crystallography data

The structure of Crystal Structure of the Highly Conserved Rna Internal Loop of Srp, PDB code: 1lnt was solved by J.Deng, Y.Xiong, B.Pan, M.Sundaralingam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.70
Space group P 43 2 2
Cell size a, b, c (Å), α, β, γ (°) 35.610, 35.610, 133.960, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 22.5

Other elements in 1lnt:

The structure of Crystal Structure of the Highly Conserved Rna Internal Loop of Srp also contains other interesting chemical elements:

Bromine (Br) 2 atoms
Calcium (Ca) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Highly Conserved Rna Internal Loop of Srp (pdb code 1lnt). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the Highly Conserved Rna Internal Loop of Srp, PDB code: 1lnt:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1lnt

Go back to Magnesium Binding Sites List in 1lnt
Magnesium binding site 1 out of 4 in the Crystal Structure of the Highly Conserved Rna Internal Loop of Srp


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 the Highly Conserved Rna Internal Loop of Srp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg102

b:39.5
occ:0.50
O A:HOH280 1.9 47.5 1.0
O A:HOH208 2.0 44.3 1.0
OP1 A:U9 3.9 39.8 1.0
OP2 A:C10 4.5 25.3 1.0
O A:HOH311 4.9 46.7 1.0

Magnesium binding site 2 out of 4 in 1lnt

Go back to Magnesium Binding Sites List in 1lnt
Magnesium binding site 2 out of 4 in the Crystal Structure of the Highly Conserved Rna Internal Loop of Srp


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 the Highly Conserved Rna Internal Loop of Srp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg103

b:43.2
occ:1.00
O A:HOH270 2.1 47.9 1.0
O B:HOH271 2.3 58.8 1.0
O B:HOH308 2.5 45.9 1.0
O B:HOH260 2.6 41.9 1.0
O A:HOH291 3.8 55.1 1.0
OP2 A:C5 4.0 33.9 1.0
O A:HOH244 4.1 40.6 1.0
O B:HOH237 4.1 38.3 1.0
O B:HOH225 4.4 39.5 1.0
OP2 B:A17 4.6 29.4 1.0

Magnesium binding site 3 out of 4 in 1lnt

Go back to Magnesium Binding Sites List in 1lnt
Magnesium binding site 3 out of 4 in the Crystal Structure of the Highly Conserved Rna Internal Loop of Srp


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 the Highly Conserved Rna Internal Loop of Srp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg104

b:42.0
occ:1.00
O A:HOH220 2.0 30.4 1.0
O A:HOH234 2.2 34.5 1.0
O A:HOH243 2.2 35.4 1.0
O A:HOH245 2.5 38.3 1.0
CA A:CA113 4.0 23.4 0.5
O6 A:G12 4.1 24.0 1.0
O A:HOH233 4.2 41.2 1.0
O A:HOH265 4.3 43.6 1.0
N7 A:G12 4.4 19.0 1.0
O A:HOH309 4.5 32.2 1.0
BR A:CBV11 4.6 26.1 1.0
C6 A:G12 4.9 22.0 1.0

Magnesium binding site 4 out of 4 in 1lnt

Go back to Magnesium Binding Sites List in 1lnt
Magnesium binding site 4 out of 4 in the Crystal Structure of the Highly Conserved Rna Internal Loop of Srp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of the Highly Conserved Rna Internal Loop of Srp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg101

b:41.6
occ:1.00
O B:HOH269 1.9 55.3 1.0
O B:HOH255 2.0 53.2 1.0
O B:HOH250 2.1 44.6 1.0
O B:HOH272 2.6 47.8 1.0
O6 B:G15 4.1 25.1 1.0
N7 B:G15 4.2 24.4 1.0
O B:HOH304 4.5 43.6 1.0
N7 B:G14 4.6 25.6 1.0
O6 B:G14 4.7 22.9 1.0
C6 B:G15 4.9 23.5 1.0
C5 B:G15 5.0 23.6 1.0

Reference:

J.Deng, Y.Xiong, B.Pan, M.Sundaralingam. Structure of An Rna Dodecamer Containing A Fragment From Srp Domain IV of Escherichia Coli. Acta Crystallogr.,Sect.D V. 59 1004 2003.
ISSN: ISSN 0907-4449
PubMed: 12777762
DOI: 10.1107/S0907444903006747
Page generated: Tue Aug 13 08:32:48 2024

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