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Atomistry » Magnesium » PDB 7bdj-7bph » 7bgn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 7bdj-7bph » 7bgn » |
Magnesium in PDB 7bgn: Crystal Structure of MTHISN2-Amp Complex, A Bifunctional Enzyme From the Histidine Biosynthetic PathwayEnzymatic activity of Crystal Structure of MTHISN2-Amp Complex, A Bifunctional Enzyme From the Histidine Biosynthetic Pathway
All present enzymatic activity of Crystal Structure of MTHISN2-Amp Complex, A Bifunctional Enzyme From the Histidine Biosynthetic Pathway:
3.5.4.19; 3.6.1.31; Protein crystallography data
The structure of Crystal Structure of MTHISN2-Amp Complex, A Bifunctional Enzyme From the Histidine Biosynthetic Pathway, PDB code: 7bgn
was solved by
W.Witek,
M.Ruszkowski,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7bgn:
The structure of Crystal Structure of MTHISN2-Amp Complex, A Bifunctional Enzyme From the Histidine Biosynthetic Pathway also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of MTHISN2-Amp Complex, A Bifunctional Enzyme From the Histidine Biosynthetic Pathway
(pdb code 7bgn). 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 MTHISN2-Amp Complex, A Bifunctional Enzyme From the Histidine Biosynthetic Pathway, PDB code: 7bgn: Magnesium binding site 1 out of 1 in 7bgnGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Crystal Structure of MTHISN2-Amp Complex, A Bifunctional Enzyme From the Histidine Biosynthetic Pathway
![]() Mono view ![]() Stereo pair view
Reference:
W.Witek,
J.Sliwiak,
M.Ruszkowski.
Structural and Mechanistic Insights Into the Bifunctional HISN2 Enzyme Catalyzing the Second and Third Steps of Histidine Biosynthesis in Plants. Sci Rep V. 11 9647 2021.
Page generated: Wed Oct 2 10:26:39 2024
ISSN: ESSN 2045-2322 PubMed: 33958623 DOI: 10.1038/S41598-021-88920-2 |
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