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Atomistry » Magnesium » PDB 2o56-2oh6 » 2ode » |
Magnesium in PDB 2ode: Crystal Structure of the Heterodimeric Complex of Human RGS8 and Activated Gi Alpha 3Protein crystallography data
The structure of Crystal Structure of the Heterodimeric Complex of Human RGS8 and Activated Gi Alpha 3, PDB code: 2ode
was solved by
C.Gileadi,
M.Soundararajan,
A.P.Turnbull,
J.M.Elkins,
E.Papagrigoriou,
A.C.W.Pike,
G.Bunkoczi,
F.Gorrec,
C.Umeano,
F.Von Delft,
J.Weigelt,
A.Edwards,
C.H.Arrowsmith,
M.Sundstrom,
D.A.Doyle,
Structural Genomicsconsortium (Sgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2ode:
The structure of Crystal Structure of the Heterodimeric Complex of Human RGS8 and Activated Gi Alpha 3 also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of the Heterodimeric Complex of Human RGS8 and Activated Gi Alpha 3
(pdb code 2ode). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Heterodimeric Complex of Human RGS8 and Activated Gi Alpha 3, PDB code: 2ode: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 2odeGo back to![]() ![]()
Magnesium binding site 1 out
of 2 in the Crystal Structure of the Heterodimeric Complex of Human RGS8 and Activated Gi Alpha 3
![]() Mono view ![]() Stereo pair view
Magnesium binding site 2 out of 2 in 2odeGo back to![]() ![]()
Magnesium binding site 2 out
of 2 in the Crystal Structure of the Heterodimeric Complex of Human RGS8 and Activated Gi Alpha 3
![]() Mono view ![]() Stereo pair view
Reference:
M.Soundararajan,
F.S.Willard,
A.J.Kimple,
A.P.Turnbull,
L.J.Ball,
G.A.Schoch,
C.Gileadi,
O.Y.Fedorov,
E.F.Dowler,
V.A.Higman,
S.Q.Hutsell,
M.Sundstrom,
D.A.Doyle,
D.P.Siderovski.
Structural Diversity in the Rgs Domain and Its Interaction with Heterotrimeric G Protein Alpha-Subunits. Proc.Natl.Acad.Sci.Usa V. 105 6457 2008.
Page generated: Wed Aug 14 01:26:13 2024
ISSN: ISSN 0027-8424 PubMed: 18434541 DOI: 10.1073/PNAS.0801508105 |
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