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Magnesium in PDB 5ixt: The Crystal Structure of the Arabidopsis Receptor Kinase Haesa Lrr Ectdomain in Complex with A N-Terminal Extended Ida Peptide Hormone Ligand.

Enzymatic activity of The Crystal Structure of the Arabidopsis Receptor Kinase Haesa Lrr Ectdomain in Complex with A N-Terminal Extended Ida Peptide Hormone Ligand.

All present enzymatic activity of The Crystal Structure of the Arabidopsis Receptor Kinase Haesa Lrr Ectdomain in Complex with A N-Terminal Extended Ida Peptide Hormone Ligand.:
2.7.10.1; 2.7.11.1;

Protein crystallography data

The structure of The Crystal Structure of the Arabidopsis Receptor Kinase Haesa Lrr Ectdomain in Complex with A N-Terminal Extended Ida Peptide Hormone Ligand., PDB code: 5ixt was solved by J.Santiago, M.Hothorn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 128.97 / 1.94
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 148.921, 148.921, 58.022, 90.00, 90.00, 120.00
R / Rfree (%) 17.9 / 20.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Crystal Structure of the Arabidopsis Receptor Kinase Haesa Lrr Ectdomain in Complex with A N-Terminal Extended Ida Peptide Hormone Ligand. (pdb code 5ixt). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Crystal Structure of the Arabidopsis Receptor Kinase Haesa Lrr Ectdomain in Complex with A N-Terminal Extended Ida Peptide Hormone Ligand., PDB code: 5ixt:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5ixt

Go back to Magnesium Binding Sites List in 5ixt
Magnesium binding site 1 out of 2 in the The Crystal Structure of the Arabidopsis Receptor Kinase Haesa Lrr Ectdomain in Complex with A N-Terminal Extended Ida Peptide Hormone Ligand.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of the Arabidopsis Receptor Kinase Haesa Lrr Ectdomain in Complex with A N-Terminal Extended Ida Peptide Hormone Ligand. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg714

b:83.8
occ:1.00
OG A:SER326 2.9 76.9 1.0
CB A:SER326 3.4 76.1 1.0
N A:SER326 3.6 75.4 1.0
CB A:PRO324 3.8 72.8 1.0
N A:ASN303 3.8 79.1 1.0
CB A:ASP302 3.9 83.8 1.0
N A:GLU325 4.0 74.9 1.0
CA A:SER326 4.1 76.0 1.0
C A:PRO324 4.4 73.0 1.0
CA A:PRO324 4.4 73.4 1.0
CA A:ASP302 4.5 83.4 1.0
CA A:ASN303 4.5 81.0 1.0
C A:GLU325 4.6 79.5 1.0
CA A:GLU325 4.6 78.0 1.0
CB A:GLU325 4.6 86.3 1.0
C A:ASP302 4.6 80.1 1.0
ND2 A:ASN303 4.7 94.2 1.0
CG A:ASP302 4.9 93.0 1.0

Magnesium binding site 2 out of 2 in 5ixt

Go back to Magnesium Binding Sites List in 5ixt
Magnesium binding site 2 out of 2 in the The Crystal Structure of the Arabidopsis Receptor Kinase Haesa Lrr Ectdomain in Complex with A N-Terminal Extended Ida Peptide Hormone Ligand.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Crystal Structure of the Arabidopsis Receptor Kinase Haesa Lrr Ectdomain in Complex with A N-Terminal Extended Ida Peptide Hormone Ligand. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg715

b:71.7
occ:1.00
OG A:SER459 3.0 72.2 0.2
OG A:SER459 3.2 82.6 0.8
OG A:SER481 3.2 81.4 1.0
CB A:SER459 3.4 81.3 0.8
CB A:SER459 3.5 75.8 0.2
N A:SER459 3.5 74.3 1.0
CB A:ARG457 3.5 72.4 1.0
CA A:ARG457 3.6 74.5 1.0
C A:ARG457 3.6 76.6 1.0
N A:ILE458 3.6 75.1 1.0
CB A:SER435 3.6 79.8 1.0
CB A:SER481 3.7 80.1 1.0
O A:SER481 3.8 75.8 1.0
OG A:SER435 3.9 78.5 1.0
CA A:SER459 4.1 76.8 0.8
CA A:SER459 4.1 75.8 0.2
CG A:ARG457 4.1 71.1 1.0
O A:ARG457 4.2 74.8 1.0
C A:SER481 4.4 84.6 1.0
C A:ILE458 4.5 76.3 1.0
CA A:ILE458 4.5 76.8 1.0
CA A:SER481 4.7 79.7 1.0
CD A:ARG457 4.9 75.3 1.0
CA A:SER435 5.0 74.4 1.0
N A:ARG457 5.0 72.0 1.0

Reference:

J.Santiago, B.Brandt, M.Wildhagen, U.Hohmann, L.A.Hothorn, M.A.Butenko, M.Hothorn. Mechanistic Insight Into A Peptide Hormone Signaling Complex Mediating Floral Organ Abscission. Elife V. 5 2016.
ISSN: ESSN 2050-084X
PubMed: 27058169
DOI: 10.7554/ELIFE.15075
Page generated: Sun Sep 29 17:07:21 2024

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