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Magnesium in PDB 8hq9: Crystal Structure of the Mlad Domain of the Mlad Protein From Escherichia Coli (Form II)

Protein crystallography data

The structure of Crystal Structure of the Mlad Domain of the Mlad Protein From Escherichia Coli (Form II), PDB code: 8hq9 was solved by A.Dutta, S.P.Kanaujia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 78.98 / 2.70
Space group P 21 2 21
Cell size a, b, c (Å), α, β, γ (°) 60.42, 106.95, 117.12, 90, 90, 90
R / Rfree (%) 20.4 / 26.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Mlad Domain of the Mlad Protein From Escherichia Coli (Form II) (pdb code 8hq9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Mlad Domain of the Mlad Protein From Escherichia Coli (Form II), PDB code: 8hq9:

Magnesium binding site 1 out of 1 in 8hq9

Go back to Magnesium Binding Sites List in 8hq9
Magnesium binding site 1 out of 1 in the Crystal Structure of the Mlad Domain of the Mlad Protein From Escherichia Coli (Form II)


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 Mlad Domain of the Mlad Protein From Escherichia Coli (Form II) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg201

b:39.4
occ:1.00
OG1 D:THR137 2.7 40.2 1.0
O D:THR45 2.7 28.2 1.0
O D:HOH304 2.9 26.9 1.0
O D:HOH317 3.1 48.0 1.0
O D:GLN135 3.2 46.2 1.0
CG2 D:THR137 3.7 38.6 1.0
CB D:THR137 3.8 39.0 1.0
C D:THR45 3.9 27.7 1.0
C D:GLN135 4.3 43.1 1.0
CB D:THR45 4.5 28.7 1.0
N D:THR137 4.5 39.5 1.0
CA D:THR45 4.5 27.5 1.0
N D:THR45 4.6 26.2 1.0
O D:HOH318 4.7 21.4 1.0
CA D:THR137 4.7 38.2 1.0
CG2 D:THR45 4.9 29.8 1.0
O D:HOH302 4.9 18.5 1.0
N D:PHE46 4.9 27.8 1.0
CA D:GLN135 4.9 43.5 1.0
O D:ILE134 4.9 34.3 1.0

Reference:

A.Dutta, S.P.Kanaujia. The Structural Features of Mlad Illuminate Its Unique Ligand-Transporting Mechanism and Ancestry To Be Published.
Page generated: Fri Oct 4 08:12:57 2024

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