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Magnesium in PDB 1zh4: Crystal Structure of the Mg+2/BEF3-Bound Receiver Domain of Kdp Potassium Transport System Response Regulator Kdpe

Protein crystallography data

The structure of Crystal Structure of the Mg+2/BEF3-Bound Receiver Domain of Kdp Potassium Transport System Response Regulator Kdpe, PDB code: 1zh4 was solved by A.Toro-Roman, T.Wu, A.M.Stock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 70.912, 126.675, 62.655, 90.00, 90.00, 90.00
R / Rfree (%) 22.7 / 26.5

Other elements in 1zh4:

The structure of Crystal Structure of the Mg+2/BEF3-Bound Receiver Domain of Kdp Potassium Transport System Response Regulator Kdpe also contains other interesting chemical elements:

Fluorine (F) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Mg+2/BEF3-Bound Receiver Domain of Kdp Potassium Transport System Response Regulator Kdpe (pdb code 1zh4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Mg+2/BEF3-Bound Receiver Domain of Kdp Potassium Transport System Response Regulator Kdpe, PDB code: 1zh4:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1zh4

Go back to Magnesium Binding Sites List in 1zh4
Magnesium binding site 1 out of 2 in the Crystal Structure of the Mg+2/BEF3-Bound Receiver Domain of Kdp Potassium Transport System Response Regulator Kdpe


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 Mg+2/BEF3-Bound Receiver Domain of Kdp Potassium Transport System Response Regulator Kdpe within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:60.7
occ:1.00
OD1 A:ASP9 1.9 59.2 1.0
O A:HOH352 2.0 44.9 1.0
F1 A:BEF301 2.1 42.3 1.0
O A:GLY54 2.2 59.4 1.0
OD2 A:ASP52 2.3 51.5 1.0
CG A:ASP9 2.9 59.4 1.0
OD2 A:ASP9 3.2 60.6 1.0
C A:GLY54 3.3 59.2 1.0
BE A:BEF301 3.3 43.6 1.0
CG A:ASP52 3.4 50.3 1.0
OD1 A:ASP52 3.7 48.9 1.0
CA A:GLY54 3.9 58.2 1.0
OE2 A:GLU8 3.9 46.9 1.0
F3 A:BEF301 4.3 43.8 1.0
CB A:ASP9 4.3 57.7 1.0
N A:GLY54 4.3 56.4 1.0
F2 A:BEF301 4.4 43.1 1.0
O A:HOH351 4.4 53.7 1.0
OE2 A:GLU10 4.4 63.0 1.0
N A:LEU55 4.4 60.6 1.0
OE1 A:GLU8 4.5 44.5 1.0
N A:ASP9 4.5 51.3 1.0
CD A:GLU8 4.6 46.3 1.0
CB A:ASP52 4.7 50.9 1.0
NZ A:LYS101 4.7 42.3 1.0
CA A:LEU55 4.8 61.9 1.0
CA A:ASP9 4.9 55.5 1.0
CD2 A:LEU55 4.9 60.6 1.0

Magnesium binding site 2 out of 2 in 1zh4

Go back to Magnesium Binding Sites List in 1zh4
Magnesium binding site 2 out of 2 in the Crystal Structure of the Mg+2/BEF3-Bound Receiver Domain of Kdp Potassium Transport System Response Regulator Kdpe


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 Mg+2/BEF3-Bound Receiver Domain of Kdp Potassium Transport System Response Regulator Kdpe within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg202

b:36.7
occ:1.00
OD1 B:ASP9 2.1 37.5 1.0
O B:GLY54 2.1 33.3 1.0
O B:HOH357 2.1 35.7 1.0
OD2 B:ASP52 2.2 33.1 1.0
O B:HOH358 2.2 27.0 1.0
F1 B:BEF302 2.2 35.0 1.0
CG B:ASP9 3.1 35.5 1.0
CG B:ASP52 3.1 31.8 1.0
BE B:BEF302 3.2 36.8 1.0
C B:GLY54 3.2 31.9 1.0
OD1 B:ASP52 3.2 32.2 1.0
OD2 B:ASP9 3.3 32.1 1.0
OE2 B:GLU8 3.7 40.3 1.0
CA B:GLY54 3.8 29.9 1.0
F3 B:BEF302 4.0 39.0 1.0
N B:GLY54 4.1 30.0 1.0
N B:LEU55 4.3 33.9 1.0
F2 B:BEF302 4.4 37.1 1.0
CB B:ASP9 4.4 35.4 1.0
CB B:ASP52 4.5 30.5 1.0
OE2 B:GLU10 4.5 41.2 1.0
CD B:GLU8 4.5 40.1 1.0
N B:ASP9 4.5 38.5 1.0
CD2 B:LEU55 4.6 33.4 1.0
CA B:LEU55 4.7 34.5 1.0
NZ B:LYS101 4.8 31.5 1.0
OE1 B:GLU8 4.8 39.6 1.0
CG B:GLU10 5.0 39.8 1.0

Reference:

A.Toro-Roman, T.Wu, A.M.Stock. A Common Dimerization Interface in Bacterial Response Regulators Kdpe and Torr. Protein Sci. V. 14 3077 2005.
ISSN: ISSN 0961-8368
PubMed: 16322582
DOI: 10.1110/PS.051722805
Page generated: Mon Dec 14 07:11:57 2020

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