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Magnesium in PDB 6rms: The Structure of Variant D274E of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp

Enzymatic activity of The Structure of Variant D274E of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp

All present enzymatic activity of The Structure of Variant D274E 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 Variant D274E of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp, PDB code: 6rms was solved by J.Krausze, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.54 / 1.74
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 64.836, 119.480, 136.867, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 22

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Structure of Variant D274E of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp (pdb code 6rms). 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 Variant D274E of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp, PDB code: 6rms:

Magnesium binding site 1 out of 1 in 6rms

Go back to Magnesium Binding Sites List in 6rms
Magnesium binding site 1 out of 1 in the The Structure of Variant D274E 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 Variant D274E 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:Mg505

b:33.0
occ:1.00
 O2P A:AMP504 1.9 24.2 1.0
O A:HOH680 2.1 28.5 1.0
O A:HOH766 2.2 29.4 1.0
O A:HOH615 2.2 26.1 1.0
O A:HOH656 2.2 27.9 1.0
H A:GLY267 3.1 36.0 1.0
P A:AMP504 3.2 32.6 1.0
O1P A:AMP504 3.7 36.3 1.0
O5' A:AMP504 3.7 33.6 1.0
H8 A:AMP504 3.7 31.2 1.0
H2' A:AMP504 3.8 30.9 1.0
HA2 A:GLY199 3.8 30.2 1.0
N A:GLY267 4.0 36.0 1.0
OE2 A:GLU201 4.0 31.2 1.0
HA3 A:GLY266 4.1 30.3 1.0
HA2 A:GLY267 4.1 37.2 1.0
O A:THR198 4.2 26.4 1.0
OE1 A:GLU201 4.2 30.5 1.0
HA3 A:GLY199 4.3 30.0 1.0
OD1 A:ASP242 4.3 37.1 1.0
OD2 A:ASP242 4.4 32.2 1.0
O A:HOH729 4.5 53.0 1.0
O3P A:AMP504 4.5 35.0 1.0
CA A:GLY199 4.5 30.1 1.0
CD A:GLU201 4.6 44.7 1.0
CA A:GLY267 4.6 37.0 1.0
C8 A:AMP504 4.6 31.2 1.0
HA2 A:GLY266 4.7 30.5 1.0
OG1 A:THR198 4.7 30.5 1.0
CG A:ASP242 4.7 36.2 1.0
H3' A:AMP504 4.7 32.2 1.0
CA A:GLY266 4.8 30.4 1.0
C2' A:AMP504 4.9 30.9 1.0
C A:GLY266 4.9 35.8 1.0
HA3 A:GLY267 4.9 37.0 1.0
C A:THR198 4.9 29.6 1.0

Reference:

T.W.Hercher, J.Krausze, S.Hoffmeister, D.Zwerschke, T.Lindel, W.Blankenfeldt, R.R.Mendel, T.Kruse. Insights Into the CNX1E Catalyzed Mpt-Amp Hydrolysis. Biosci.Rep. V. 40 2020.
ISSN: ISSN 0144-8463
PubMed: 31860061
DOI: 10.1042/BSR20191806
Page generated: Tue Oct 1 17:26:36 2024

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