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Magnesium in PDB 6etd: The Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp

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

All present enzymatic activity of The Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp:
2.10.1.1; 2.7.7.75;

Protein crystallography data

The structure of The Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp, PDB code: 6etd was solved by J.Krausze, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.13 / 1.72
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 66.130, 123.640, 132.110, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp (pdb code 6etd). 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 The Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp, PDB code: 6etd:

Magnesium binding site 1 out of 1 in 6etd

Go back to Magnesium Binding Sites List in 6etd
Magnesium binding site 1 out of 1 in the The Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:21.8
occ:1.00
 O2P A:AMP501 2.1 19.6 1.0
O A:HOH624 2.1 18.9 1.0
O A:HOH666 2.1 18.0 1.0
O A:HOH749 2.2 18.7 1.0
O A:HOH676 2.2 22.3 1.0
H A:GLY267 3.1 17.4 0.0
P A:AMP501 3.3 24.9 1.0
HA2 A:GLY199 3.5 19.4 0.0
O1P A:AMP501 3.7 24.8 1.0
H2' A:AMP501 3.9 21.5 0.0
H8 A:AMP501 3.9 20.0 0.0
OE2 A:GLU201 3.9 24.8 1.0
O5' A:AMP501 4.0 23.6 1.0
N A:GLY267 4.0 17.3 1.0
HA3 A:GLY199 4.0 18.8 0.0
OE1 A:GLU201 4.1 21.8 1.0
O A:THR198 4.1 18.1 1.0
HA2 A:GLY267 4.1 17.1 0.0
HA3 A:GLY266 4.2 16.8 0.0
OD1 A:ASP242 4.2 24.7 1.0
CA A:GLY199 4.3 18.9 1.0
OD2 A:ASP242 4.3 25.8 1.0
CD A:GLU201 4.4 28.6 1.0
OD1 A:ASP274 4.5 26.1 1.0
O3P A:AMP501 4.5 29.3 1.0
CG A:ASP242 4.6 25.8 1.0
OG1 A:THR198 4.6 19.6 1.0
CA A:GLY267 4.6 16.6 1.0
C A:THR198 4.7 20.1 1.0
C8 A:AMP501 4.8 19.9 1.0
HA2 A:GLY266 4.8 17.2 0.0
N A:GLY199 4.8 18.6 1.0
CA A:GLY266 4.8 16.8 1.0
O A:HOH611 4.9 28.5 1.0
C A:GLY266 4.9 22.0 1.0
H3' A:AMP501 4.9 22.8 0.0
C2' A:AMP501 4.9 21.4 1.0
HA3 A:GLY267 5.0 16.5 0.0
H A:ASP200 5.0 18.5 0.0

Reference:

J.Krausze, T.W.Hercher, D.Zwerschke, M.L.Kirk, W.Blankenfeldt, R.R.Mendel, T.Kruse. The Functional Principle of Eukaryotic Molybdenum Insertases. Biochem. J. V. 475 1739 2018.
ISSN: ESSN 1470-8728
PubMed: 29717023
DOI: 10.1042/BCJ20170935
Page generated: Tue Oct 1 00:01:41 2024

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