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Magnesium in PDB 7pxy: Crystal Structure of Arabidopsis Thaliana 5-Enol-Pyruvyl-Shikimate-3- Phosphate Synthase (Epsps) in Open ConformationEnzymatic activity of Crystal Structure of Arabidopsis Thaliana 5-Enol-Pyruvyl-Shikimate-3- Phosphate Synthase (Epsps) in Open Conformation
All present enzymatic activity of Crystal Structure of Arabidopsis Thaliana 5-Enol-Pyruvyl-Shikimate-3- Phosphate Synthase (Epsps) in Open Conformation:
2.5.1.19; Protein crystallography data
The structure of Crystal Structure of Arabidopsis Thaliana 5-Enol-Pyruvyl-Shikimate-3- Phosphate Synthase (Epsps) in Open Conformation, PDB code: 7pxy
was solved by
M.Ruszkowski,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7pxy:
The structure of Crystal Structure of Arabidopsis Thaliana 5-Enol-Pyruvyl-Shikimate-3- Phosphate Synthase (Epsps) in Open Conformation also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Arabidopsis Thaliana 5-Enol-Pyruvyl-Shikimate-3- Phosphate Synthase (Epsps) in Open Conformation
(pdb code 7pxy). 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 Arabidopsis Thaliana 5-Enol-Pyruvyl-Shikimate-3- Phosphate Synthase (Epsps) in Open Conformation, PDB code: 7pxy: Magnesium binding site 1 out of 1 in 7pxyGo back to Magnesium Binding Sites List in 7pxy
Magnesium binding site 1 out
of 1 in the Crystal Structure of Arabidopsis Thaliana 5-Enol-Pyruvyl-Shikimate-3- Phosphate Synthase (Epsps) in Open Conformation
Mono view Stereo pair view
Reference:
M.Ruszkowski,
G.Forlani.
Deciphering the Structure of Arabidopsis Thaliana 5- Enol -Pyruvyl-Shikimate-3-Phosphate Synthase: An Essential Step Toward the Discovery of Novel Inhibitors to Supersede Glyphosate. Comput Struct Biotechnol J V. 20 1494 2022.
Page generated: Thu Oct 3 04:51:41 2024
ISSN: ESSN 2001-0370 PubMed: 35422967 DOI: 10.1016/J.CSBJ.2022.03.020 |
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