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Atomistry » Sodium » PDB 1t4b-1u8r » 1tk6 » |
Sodium in PDB 1tk6: Iron-Oxo Clusters Biomineralizing on Protein Surfaces. Structural Analysis of H.Salinarum Dpsa in Its Low and High Iron StatesProtein crystallography data
The structure of Iron-Oxo Clusters Biomineralizing on Protein Surfaces. Structural Analysis of H.Salinarum Dpsa in Its Low and High Iron States, PDB code: 1tk6
was solved by
K.Zeth,
S.Offermann,
L.O.Essen,
D.Oesterhelt,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1tk6:
The structure of Iron-Oxo Clusters Biomineralizing on Protein Surfaces. Structural Analysis of H.Salinarum Dpsa in Its Low and High Iron States also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Iron-Oxo Clusters Biomineralizing on Protein Surfaces. Structural Analysis of H.Salinarum Dpsa in Its Low and High Iron States
(pdb code 1tk6). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Iron-Oxo Clusters Biomineralizing on Protein Surfaces. Structural Analysis of H.Salinarum Dpsa in Its Low and High Iron States, PDB code: 1tk6: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 1tk6Go back to![]() ![]()
Sodium binding site 1 out
of 2 in the Iron-Oxo Clusters Biomineralizing on Protein Surfaces. Structural Analysis of H.Salinarum Dpsa in Its Low and High Iron States
![]() Mono view ![]() Stereo pair view
Sodium binding site 2 out of 2 in 1tk6Go back to![]() ![]()
Sodium binding site 2 out
of 2 in the Iron-Oxo Clusters Biomineralizing on Protein Surfaces. Structural Analysis of H.Salinarum Dpsa in Its Low and High Iron States
![]() Mono view ![]() Stereo pair view
Reference:
K.Zeth,
S.Offermann,
L.O.Essen,
D.Oesterhelt.
Iron-Oxo Clusters Biomineralizing on Protein Surfaces: Structural Analysis of Halobacterium Salinarum Dpsa in Its Low- and High-Iron States. Proc.Natl.Acad.Sci.Usa V. 101 13780 2004.
Page generated: Sun Oct 6 22:39:56 2024
ISSN: ISSN 0027-8424 PubMed: 15365182 DOI: 10.1073/PNAS.0401821101 |
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