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Atomistry » Yttrium » PDB 3ph6-8pun » 3ph6 » |
Yttrium in PDB 3ph6: Bovine Beta Lactoglobulin Crytsallized Through Ligandation of YttriumProtein crystallography data
The structure of Bovine Beta Lactoglobulin Crytsallized Through Ligandation of Yttrium, PDB code: 3ph6
was solved by
G.Zocher,
T.Stehle,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3ph6:
The structure of Bovine Beta Lactoglobulin Crytsallized Through Ligandation of Yttrium also contains other interesting chemical elements:
Yttrium Binding Sites:
The binding sites of Yttrium atom in the Bovine Beta Lactoglobulin Crytsallized Through Ligandation of Yttrium
(pdb code 3ph6). This binding sites where shown within
5.0 Angstroms radius around Yttrium atom.
In total 4 binding sites of Yttrium where determined in the Bovine Beta Lactoglobulin Crytsallized Through Ligandation of Yttrium, PDB code: 3ph6: Jump to Yttrium binding site number: 1; 2; 3; 4; Yttrium binding site 1 out of 4 in 3ph6Go back to Yttrium Binding Sites List in 3ph6
Yttrium binding site 1 out
of 4 in the Bovine Beta Lactoglobulin Crytsallized Through Ligandation of Yttrium
Mono view Stereo pair view
Yttrium binding site 2 out of 4 in 3ph6Go back to Yttrium Binding Sites List in 3ph6
Yttrium binding site 2 out
of 4 in the Bovine Beta Lactoglobulin Crytsallized Through Ligandation of Yttrium
Mono view Stereo pair view
Yttrium binding site 3 out of 4 in 3ph6Go back to Yttrium Binding Sites List in 3ph6
Yttrium binding site 3 out
of 4 in the Bovine Beta Lactoglobulin Crytsallized Through Ligandation of Yttrium
Mono view Stereo pair view
Yttrium binding site 4 out of 4 in 3ph6Go back to Yttrium Binding Sites List in 3ph6
Yttrium binding site 4 out
of 4 in the Bovine Beta Lactoglobulin Crytsallized Through Ligandation of Yttrium
Mono view Stereo pair view
Reference:
F.Zhang,
G.Zocher,
A.Sauter,
T.Stehle,
F.Schreiber.
Novel Approach to Protein Crystallization Through Ligandation of Yttrium Cations J.Appl.Crystallogr. V. 44 755 2011.
Page generated: Mon Jan 25 16:07:19 2021
ISSN: ISSN 0021-8898 DOI: 10.1107/S0021889811017997 |
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