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Atomistry » Sodium » PDB 3k9g-3la1 » 3l1o » |
Sodium in PDB 3l1o: Crystal Structure of Monoclonal Antibody MN423 Fab Fragment with Free Combining Site, Crystallized in the Presence of ZincProtein crystallography data
The structure of Crystal Structure of Monoclonal Antibody MN423 Fab Fragment with Free Combining Site, Crystallized in the Presence of Zinc, PDB code: 3l1o
was solved by
R.Skrabana,
J.Sevcik,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3l1o:
The structure of Crystal Structure of Monoclonal Antibody MN423 Fab Fragment with Free Combining Site, Crystallized in the Presence of Zinc also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Monoclonal Antibody MN423 Fab Fragment with Free Combining Site, Crystallized in the Presence of Zinc
(pdb code 3l1o). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of Monoclonal Antibody MN423 Fab Fragment with Free Combining Site, Crystallized in the Presence of Zinc, PDB code: 3l1o: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 3l1oGo back to Sodium Binding Sites List in 3l1o
Sodium binding site 1 out
of 2 in the Crystal Structure of Monoclonal Antibody MN423 Fab Fragment with Free Combining Site, Crystallized in the Presence of Zinc
Mono view Stereo pair view
Sodium binding site 2 out of 2 in 3l1oGo back to Sodium Binding Sites List in 3l1o
Sodium binding site 2 out
of 2 in the Crystal Structure of Monoclonal Antibody MN423 Fab Fragment with Free Combining Site, Crystallized in the Presence of Zinc
Mono view Stereo pair view
Reference:
R.Skrabana,
R.Dvorsky,
J.Sevcik,
M.Novak.
Monoclonal Antibody MN423 As A Stable Mold Facilitates Structure Determination of Disordered Tau Protein J.Struct.Biol. V. 171 74 2010.
Page generated: Mon Oct 7 11:16:25 2024
ISSN: ISSN 1047-8477 PubMed: 20184958 DOI: 10.1016/J.JSB.2010.02.016 |
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