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Atomistry » Magnesium » PDB 5xus-5y4i » 5xz8 » |
Magnesium in PDB 5xz8: Crystal Structure of Phosphofructokinase From Staphylococcus Aureus in Complex with Adenylylimidodiphosphate (the Atp Analog) and Fructose- 6-PhosphateEnzymatic activity of Crystal Structure of Phosphofructokinase From Staphylococcus Aureus in Complex with Adenylylimidodiphosphate (the Atp Analog) and Fructose- 6-Phosphate
All present enzymatic activity of Crystal Structure of Phosphofructokinase From Staphylococcus Aureus in Complex with Adenylylimidodiphosphate (the Atp Analog) and Fructose- 6-Phosphate:
2.7.1.11; Protein crystallography data
The structure of Crystal Structure of Phosphofructokinase From Staphylococcus Aureus in Complex with Adenylylimidodiphosphate (the Atp Analog) and Fructose- 6-Phosphate, PDB code: 5xz8
was solved by
C.L.Wang,
T.Tian,
J.Y.Zang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Phosphofructokinase From Staphylococcus Aureus in Complex with Adenylylimidodiphosphate (the Atp Analog) and Fructose- 6-Phosphate
(pdb code 5xz8). 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 Phosphofructokinase From Staphylococcus Aureus in Complex with Adenylylimidodiphosphate (the Atp Analog) and Fructose- 6-Phosphate, PDB code: 5xz8: Magnesium binding site 1 out of 1 in 5xz8Go back to Magnesium Binding Sites List in 5xz8
Magnesium binding site 1 out
of 1 in the Crystal Structure of Phosphofructokinase From Staphylococcus Aureus in Complex with Adenylylimidodiphosphate (the Atp Analog) and Fructose- 6-Phosphate
Mono view Stereo pair view
Reference:
T.Tian,
C.L.Wang,
M.H.Wu,
X.Zhang,
J.Y.Zang.
Structural Insights Into the Regulation of Staphylococcus Aureus Phosphofructokinase By Tetramer-Dimer Conversion. Biochemistry V. 57 4252 2018.
Page generated: Mon Sep 30 10:39:48 2024
ISSN: ISSN 1520-4995 PubMed: 29940104 DOI: 10.1021/ACS.BIOCHEM.8B00028 |
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