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Atomistry » Magnesium » PDB 2fl6-2fwq » 2fwn | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 2fl6-2fwq » 2fwn » |
Magnesium in PDB 2fwn: Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate InactivationEnzymatic activity of Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation
All present enzymatic activity of Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation:
4.1.1.7; Protein crystallography data
The structure of Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation, PDB code: 2fwn
was solved by
A.K.Bera,
M.S.Hasson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2fwn:
The structure of Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation
(pdb code 2fwn). 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 Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation, PDB code: 2fwn: Magnesium binding site 1 out of 1 in 2fwnGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation
![]() Mono view ![]() Stereo pair view
Reference:
A.K.Bera,
L.S.Polovnikova,
J.Roestamadji,
T.S.Widlanski,
G.L.Kenyon,
M.J.Mcleish,
M.S.Hasson.
Mechanism-Based Inactivation of Benzoylformate Decarboxylase, A Thiamin Diphosphate-Dependent Enzyme J.Am.Chem.Soc. V. 129 4120 2007.
Page generated: Tue Aug 13 23:19:28 2024
ISSN: ISSN 0002-7863 PubMed: 17367138 DOI: 10.1021/JA068636Z |
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