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Atomistry » Sodium » PDB 1m90-1nji » 1mg2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 1m90-1nji » 1mg2 » |
Sodium in PDB 1mg2: Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with AmicyaninEnzymatic activity of Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin
All present enzymatic activity of Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin:
1.4.99.3; Protein crystallography data
The structure of Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin, PDB code: 1mg2
was solved by
D.Sun,
Z.W.Chen,
F.S.Mathews,
V.L.Davidson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1mg2:
The structure of Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin
(pdb code 1mg2). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 4 binding sites of Sodium where determined in the Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin, PDB code: 1mg2: Jump to Sodium binding site number: 1; 2; 3; 4; Sodium binding site 1 out of 4 in 1mg2Go back to Sodium Binding Sites List in 1mg2
Sodium binding site 1 out
of 4 in the Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin
Mono view Stereo pair view
Sodium binding site 2 out of 4 in 1mg2Go back to Sodium Binding Sites List in 1mg2
Sodium binding site 2 out
of 4 in the Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin
Mono view Stereo pair view
Sodium binding site 3 out of 4 in 1mg2Go back to Sodium Binding Sites List in 1mg2
Sodium binding site 3 out
of 4 in the Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin
Mono view Stereo pair view
Sodium binding site 4 out of 4 in 1mg2Go back to Sodium Binding Sites List in 1mg2
Sodium binding site 4 out
of 4 in the Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin
Mono view Stereo pair view
Reference:
D.Sun,
Z.W.Chen,
F.S.Mathews,
V.L.Davidson.
Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin Biochemistry V. 41 13926 2002.
Page generated: Sun Oct 6 20:31:32 2024
ISSN: ISSN 0006-2960 PubMed: 12437349 DOI: 10.1021/BI026654X |
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