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Magnesium in PDB 2a6e: Crystal Structure of the T. Thermophilus Rna Polymerase HoloenzymeEnzymatic activity of Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme
All present enzymatic activity of Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme:
2.7.7.6; Protein crystallography data
The structure of Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme, PDB code: 2a6e
was solved by
I.Artsimovitch,
M.N.Vassylyeva,
D.Svetlov,
V.Svetlov,
A.Perederina,
N.Igarashi,
N.Matsugaki,
S.Wakatsuki,
T.H.Tahirov,
D.G.Vassylyev,
Riken Structural Genomics/Proteomicsinitiative (Rsgi),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2a6e:
The structure of Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme
(pdb code 2a6e). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme, PDB code: 2a6e: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 2a6eGo back to Magnesium Binding Sites List in 2a6e
Magnesium binding site 1 out
of 2 in the Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 2a6eGo back to Magnesium Binding Sites List in 2a6e
Magnesium binding site 2 out
of 2 in the Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme
Mono view Stereo pair view
Reference:
I.Artsimovitch,
M.N.Vassylyeva,
D.Svetlov,
V.Svetlov,
A.Perederina,
N.Igarashi,
N.Matsugaki,
S.Wakatsuki,
T.H.Tahirov,
D.G.Vassylyev.
Allosteric Modulation of the Rna Polymerase Catalytic Reaction Is An Essential Component of Transcription Control By Rifamycins. Cell(Cambridge,Mass.) V. 122 351 2005.
Page generated: Mon Dec 14 07:14:48 2020
ISSN: ISSN 0092-8674 PubMed: 16096056 DOI: 10.1016/J.CELL.2005.07.014 |
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