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Atomistry » Chlorine » PDB 1xkk-1y6p » 1xmk | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 1xkk-1y6p » 1xmk » |
Chlorine in PDB 1xmk: The Crystal Structure of the Zb Domain From the Rna Editing Enzyme ADAR1Protein crystallography data
The structure of The Crystal Structure of the Zb Domain From the Rna Editing Enzyme ADAR1, PDB code: 1xmk
was solved by
A.Athanasiadis,
D.Placido,
S.Maas,
B.A.Brown Ii,
K.Lowenhaupt,
A.Rich,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1xmk:
The structure of The Crystal Structure of the Zb Domain From the Rna Editing Enzyme ADAR1 also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the The Crystal Structure of the Zb Domain From the Rna Editing Enzyme ADAR1
(pdb code 1xmk). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the The Crystal Structure of the Zb Domain From the Rna Editing Enzyme ADAR1, PDB code: 1xmk: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 1xmkGo back to Chlorine Binding Sites List in 1xmk
Chlorine binding site 1 out
of 2 in the The Crystal Structure of the Zb Domain From the Rna Editing Enzyme ADAR1
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 1xmkGo back to Chlorine Binding Sites List in 1xmk
Chlorine binding site 2 out
of 2 in the The Crystal Structure of the Zb Domain From the Rna Editing Enzyme ADAR1
Mono view Stereo pair view
Reference:
A.Athanasiadis,
D.Placido,
S.Maas,
B.A.Brown Ii,
K.Lowenhaupt,
A.Rich.
The Crystal Structure of the Z[Beta] Domain of the Rna-Editing Enzyme ADAR1 Reveals Distinct Conserved Surfaces Among Z-Domains. J.Mol.Biol. V. 351 496 2005.
Page generated: Sat Jul 20 04:00:32 2024
ISSN: ISSN 0022-2836 PubMed: 16023667 DOI: 10.1016/J.JMB.2005.06.028 |
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