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Atomistry » Magnesium » PDB 1pi3-1q24 » 1q08 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1pi3-1q24 » 1q08 » |
Magnesium in PDB 1q08: Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator, at 1.9 A Resolution (Space Group P212121)Protein crystallography data
The structure of Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator, at 1.9 A Resolution (Space Group P212121), PDB code: 1q08
was solved by
A.Changela,
K.Chen,
Y.Xue,
J.Holschen,
C.E.Outten,
T.V.O'halloran,
A.Mondragon,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1q08:
The structure of Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator, at 1.9 A Resolution (Space Group P212121) also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator, at 1.9 A Resolution (Space Group P212121)
(pdb code 1q08). 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 Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator, at 1.9 A Resolution (Space Group P212121), PDB code: 1q08: Magnesium binding site 1 out of 1 in 1q08Go back to Magnesium Binding Sites List in 1q08
Magnesium binding site 1 out
of 1 in the Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator, at 1.9 A Resolution (Space Group P212121)
Mono view Stereo pair view
Reference:
A.Changela,
K.Chen,
Y.Xue,
J.Holschen,
C.E.Outten,
T.V.O'halloran,
A.Mondragon.
Molecular Basis of Metal-Ion Selectivity and Zeptomolar Sensitivity By Cuer Science V. 301 1383 2003.
Page generated: Tue Aug 13 10:58:46 2024
ISSN: ISSN 0036-8075 PubMed: 12958362 DOI: 10.1126/SCIENCE.1085950 |
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