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Chlorine in PDB 6gb9: The Structure of Variant S328A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp

Enzymatic activity of The Structure of Variant S328A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp

All present enzymatic activity of The Structure of Variant S328A 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 S328A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp, PDB code: 6gb9 was solved by J.Krausze, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 66.41 / 1.67
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 66.020, 123.800, 132.810, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 21.5

Other elements in 6gb9:

The structure of The Structure of Variant S328A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Structure of Variant S328A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp (pdb code 6gb9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the The Structure of Variant S328A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp, PDB code: 6gb9:

Chlorine binding site 1 out of 1 in 6gb9

Go back to Chlorine Binding Sites List in 6gb9
Chlorine binding site 1 out of 1 in the The Structure of Variant S328A of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Amp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Structure of Variant S328A 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:Cl506

b:40.9
occ:1.00
 H A:GLY296 2.3 28.6 0.0
HH12 A:ARG369 2.5 30.4 0.0
HH22 A:ARG369 2.7 40.8 0.0
HA A:PRO295 2.9 23.1 0.0
O A:HOH930 2.9 35.0 1.0
O A:HOH804 3.0 24.3 1.0
HB2 A:SER400 3.0 22.0 0.0
HB3 A:SER400 3.0 20.7 0.0
O A:HOH697 3.3 27.2 1.0
N A:GLY296 3.3 28.3 1.0
HG3 A:LYS294 3.4 34.8 0.0
NH1 A:ARG369 3.5 30.7 1.0
NH2 A:ARG369 3.6 41.2 1.0
HG A:SER400 3.6 23.0 0.0
CA A:PRO295 3.8 22.5 1.0
H A:SER400 3.9 20.8 0.0
H A:SER400 4.0 21.2 0.0
HA2 A:GLY296 4.0 27.6 0.0
CZ A:ARG369 4.0 51.1 1.0
CB A:SER400 4.0 20.3 0.5
CB A:SER400 4.0 21.6 0.5
HB3 A:PRO295 4.0 23.5 0.0
C A:PRO295 4.0 29.4 1.0
HB2 A:PRO295 4.1 23.0 0.0
CB A:PRO295 4.2 23.2 1.0
HA A:LYS294 4.2 22.8 0.0
HH11 A:ARG369 4.2 30.7 0.0
HE2 A:LYS294 4.2 57.0 0.0
CA A:GLY296 4.2 27.4 1.0
OG A:SER400 4.3 22.7 0.5
HZ3 A:LYS294 4.3 66.3 0.0
HB3 A:SER400 4.3 21.7 0.0
CG A:LYS294 4.4 34.9 1.0
HH21 A:ARG369 4.4 41.9 0.0
O A:HOH682 4.4 34.8 1.0
HG2 A:LYS294 4.4 34.4 0.0
HB2 A:SER400 4.6 19.9 0.0
N A:SER400 4.7 20.4 0.5
N A:SER400 4.7 20.8 0.5
OG A:SER400 4.7 25.4 0.5
O A:HOH949 4.7 50.0 1.0
HG A:SER400 4.9 25.4 0.0
O A:HOH986 4.9 37.2 1.0
CA A:SER400 4.9 18.6 0.5
O A:GLY296 4.9 31.8 1.0
CA A:SER400 5.0 19.2 0.5
N A:PRO295 5.0 22.8 1.0
CE A:LYS294 5.0 57.1 1.0

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: Sat Jul 12 14:29:29 2025

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