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Magnesium in PDB 2o5j: Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog
Enzymatic activity of Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog
All present enzymatic activity of Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog:
2.7.7.6;
2.7.7.6;
Protein crystallography data
The structure of Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog, PDB code: 2o5j
was solved by
D.G.Vassylyev,
M.N.Vassylyeva,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 40.00 / 3.00 |
| Space group | P 41 |
| Cell size a, b, c (Å), α, β, γ (°) | 152.340, 152.340, 524.567, 90.00, 90.00, 90.00 |
| R / Rfree (%) | 22.5 / 25.7 |
Other elements in 2o5j:
The structure of Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog also contains other interesting chemical elements:
| Zinc | (Zn) | 4 atoms |
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog
(pdb code 2o5j). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog, PDB code: 2o5j:
Jump to Magnesium binding site number: 1; 2; 3; 4;
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog, PDB code: 2o5j:
Jump to Magnesium binding site number: 1; 2; 3; 4;
Magnesium binding site 1 out of 4 in 2o5j
Go back to
Magnesium Binding Sites List in 2o5j
Magnesium binding site 1 out
of 4 in the Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog within 5.0Å range:
|
Magnesium binding site 2 out of 4 in 2o5j
Go back to
Magnesium Binding Sites List in 2o5j
Magnesium binding site 2 out
of 4 in the Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog within 5.0Å range:
|
Magnesium binding site 3 out of 4 in 2o5j
Go back to
Magnesium Binding Sites List in 2o5j
Magnesium binding site 3 out
of 4 in the Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog within 5.0Å range:
|
Magnesium binding site 4 out of 4 in 2o5j
Go back to
Magnesium Binding Sites List in 2o5j
Magnesium binding site 4 out
of 4 in the Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Crystal Structure of the T. Thermophilus Rnap Polymerase Elongation Complex with the Ntp Substrate Analog within 5.0Å range:
|
Reference:
D.G.Vassylyev,
M.N.Vassylyeva,
J.Zhang,
M.Palangat,
I.Artsimovitch,
R.Landick.
Structural Basis For Substrate Loading in Bacterial Rna Polymerase. Nature V. 448 163 2007.
ISSN: ISSN 0028-0836
PubMed: 17581591
DOI: 10.1038/NATURE05931
Page generated: Wed Aug 14 01:23:05 2024
ISSN: ISSN 0028-0836
PubMed: 17581591
DOI: 10.1038/NATURE05931
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