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Zinc in PDB 3dxj: Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin
Enzymatic activity of Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin
All present enzymatic activity of Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin:
2.7.7.6;
2.7.7.6;
Protein crystallography data
The structure of Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin, PDB code: 3dxj
was solved by
K.Das,
E.Arnold,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 50.00 / 3.00 |
| Space group | P 32 |
| Cell size a, b, c (Å), α, β, γ (°) | 235.090, 235.090, 250.880, 90.00, 90.00, 120.00 |
| R / Rfree (%) | 23.5 / 28.9 |
Other elements in 3dxj:
The structure of Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin also contains other interesting chemical elements:
| Magnesium | (Mg) | 3 atoms |
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin
(pdb code 3dxj). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin, PDB code: 3dxj:
Jump to Zinc binding site number: 1; 2; 3; 4;
In total 4 binding sites of Zinc where determined in the Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin, PDB code: 3dxj:
Jump to Zinc binding site number: 1; 2; 3; 4;
Zinc binding site 1 out of 4 in 3dxj
Go back to
Zinc Binding Sites List in 3dxj
Zinc binding site 1 out
of 4 in the Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin within 5.0Å range:
|
Zinc binding site 2 out of 4 in 3dxj
Go back to
Zinc Binding Sites List in 3dxj
Zinc binding site 2 out
of 4 in the Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin within 5.0Å range:
|
Zinc binding site 3 out of 4 in 3dxj
Go back to
Zinc Binding Sites List in 3dxj
Zinc binding site 3 out
of 4 in the Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin within 5.0Å range:
|
Zinc binding site 4 out of 4 in 3dxj
Go back to
Zinc Binding Sites List in 3dxj
Zinc binding site 4 out
of 4 in the Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of Thermus Thermophilus Rna Polymerase Holoenzyme in Complex with the Antibiotic Myxopyronin within 5.0Å range:
|
Reference:
J.Mukhopadhyay,
K.Das,
S.Ismail,
D.Koppstein,
M.Jang,
B.Hudson,
S.Sarafianos,
S.Tuske,
J.Patel,
R.Jansen,
H.Irschik,
E.Arnold,
R.H.Ebright.
The Rna Polymerase "Switch Region" Is A Target For Inhibitors. Cell(Cambridge,Mass.) V. 135 295 2008.
ISSN: ISSN 0092-8674
PubMed: 18957204
DOI: 10.1016/J.CELL.2008.09.033
Page generated: Wed Aug 20 08:36:35 2025
ISSN: ISSN 0092-8674
PubMed: 18957204
DOI: 10.1016/J.CELL.2008.09.033
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