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Atomistry » Magnesium » PDB 2vfx-2vsc » 2vpo » |
Magnesium in PDB 2vpo: High Resolution Structure of the Periplasmic Binding Protein Teaa From Teaabc Trap Transporter of Halomonas Elongata in Complex with HydroxyectoineProtein crystallography data
The structure of High Resolution Structure of the Periplasmic Binding Protein Teaa From Teaabc Trap Transporter of Halomonas Elongata in Complex with Hydroxyectoine, PDB code: 2vpo
was solved by
S.I.Kuhlmann,
A.C.Terwisscha Van Scheltinga,
R.Bienert,
H.J.Kunte,
C.Ziegler,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the High Resolution Structure of the Periplasmic Binding Protein Teaa From Teaabc Trap Transporter of Halomonas Elongata in Complex with Hydroxyectoine
(pdb code 2vpo). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the High Resolution Structure of the Periplasmic Binding Protein Teaa From Teaabc Trap Transporter of Halomonas Elongata in Complex with Hydroxyectoine, PDB code: 2vpo: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 2vpoGo back to Magnesium Binding Sites List in 2vpo
Magnesium binding site 1 out
of 2 in the High Resolution Structure of the Periplasmic Binding Protein Teaa From Teaabc Trap Transporter of Halomonas Elongata in Complex with Hydroxyectoine
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 2vpoGo back to Magnesium Binding Sites List in 2vpo
Magnesium binding site 2 out
of 2 in the High Resolution Structure of the Periplasmic Binding Protein Teaa From Teaabc Trap Transporter of Halomonas Elongata in Complex with Hydroxyectoine
Mono view Stereo pair view
Reference:
S.I.Kuhlmann,
A.C.Terwisscha Van Scheltinga,
R.Bienert,
H.J.Kunte,
C.Ziegler.
1.55 A Structure of the Ectoine Binding Protein Teaa of the Osmoregulated Trap-Transporter Teaabc From Halomonas Elongata. Biochemistry V. 47 9475 2008.
Page generated: Mon Dec 14 07:42:29 2020
ISSN: ISSN 0006-2960 PubMed: 18702523 DOI: 10.1021/BI8006719 |
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