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Atomistry » Magnesium » PDB 1nzz-1oev » 1o08 » |
Magnesium in PDB 1o08: Structure of Pentavalent Phosphorous Intermediate of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed on Cocrystallization with Glucose 1-PhosphateEnzymatic activity of Structure of Pentavalent Phosphorous Intermediate of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed on Cocrystallization with Glucose 1-Phosphate
All present enzymatic activity of Structure of Pentavalent Phosphorous Intermediate of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed on Cocrystallization with Glucose 1-Phosphate:
5.4.2.6; Protein crystallography data
The structure of Structure of Pentavalent Phosphorous Intermediate of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed on Cocrystallization with Glucose 1-Phosphate, PDB code: 1o08
was solved by
S.D.Lahiri,
G.Zhang,
D.Dunaway-Mariano,
K.N.Allen,
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 Structure of Pentavalent Phosphorous Intermediate of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed on Cocrystallization with Glucose 1-Phosphate
(pdb code 1o08). 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 Structure of Pentavalent Phosphorous Intermediate of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed on Cocrystallization with Glucose 1-Phosphate, PDB code: 1o08: Magnesium binding site 1 out of 1 in 1o08Go back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Structure of Pentavalent Phosphorous Intermediate of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed on Cocrystallization with Glucose 1-Phosphate
![]() Mono view ![]() Stereo pair view
Reference:
S.D.Lahiri,
G.Zhang,
D.Dunaway-Mariano,
K.N.Allen.
The Pentacovalent Phosphorus Intermediate of A Phosphoryl Transfer Reaction. Science V. 299 2067 2003.
Page generated: Tue Aug 13 10:30:21 2024
ISSN: ISSN 0036-8075 PubMed: 12637673 DOI: 10.1126/SCIENCE.1082710 |
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