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Magnesium in PDB 5g2s: Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate

Enzymatic activity of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate

All present enzymatic activity of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate:
2.10.1.1;

Protein crystallography data

The structure of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate, PDB code: 5g2s was solved by J.Krausze, C.Probst, T.Kruse, D.W.Heinz, R.R.Mendel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.802 / 2.84
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 65.900, 122.330, 131.620, 90.00, 90.00, 90.00
R / Rfree (%) 22.46 / 24.26

Other elements in 5g2s:

The structure of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate also contains other interesting chemical elements:

Molybdenum (Mo) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate (pdb code 5g2s). 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 Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate, PDB code: 5g2s:

Magnesium binding site 1 out of 1 in 5g2s

Go back to Magnesium Binding Sites List in 5g2s
Magnesium binding site 1 out of 1 in the Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate


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 Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1500

b:78.3
occ:1.00
 O A:HOH2002 2.1 61.1 1.0
O A:HOH2006 2.1 0.9 1.0
O A:HOH2004 2.1 66.0 1.0
O A:HOH2001 2.1 78.1 1.0
OD1 A:ASP274 4.2 85.0 1.0
OE2 A:GLU201 4.5 65.6 1.0
N A:GLY267 4.6 0.1 1.0
OD1 A:ASP242 4.7 91.5 1.0
OE1 A:GLU201 4.8 69.0 1.0
O A:HOH2005 4.8 44.6 1.0
O A:THR198 5.0 81.8 1.0

Reference:

J.Krausze, C.Probst, U.Curth, J.Reichelt, S.Saha, D.Schafflik, D.W.Heinz, R.R.Mendel, T.Kruse. Dimerization of the Plant Molybdenum Insertase CNX1E Is Required For Synthesis of the Molybdenum Cofactor. Biochem.J. V. 474 163 2017.
ISSN: ISSN 0264-6021
PubMed: 27803248
DOI: 10.1042/BCJ20160846
Page generated: Sun Sep 29 04:35:28 2024

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