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Magnesium in PDB 2ihb: Crystal Structure of the Heterodimeric Complex of Human RGS10 and Activated Gi Alpha 3

Protein crystallography data

The structure of Crystal Structure of the Heterodimeric Complex of Human RGS10 and Activated Gi Alpha 3, PDB code: 2ihb was solved by M.Soundararajan, A.P.Turnbull, E.Papagrigoriou, A.C.W.Pike, G.Bunkoczi, E.Ugochukwu, F.Gorrec, F.Von Delft, J.Weigelt, A.Edwards, C.Arrowsmith, M.Sundstrom, D.A.Doyle, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.60 / 2.71
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 100.628, 100.628, 145.359, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 23.6

Other elements in 2ihb:

The structure of Crystal Structure of the Heterodimeric Complex of Human RGS10 and Activated Gi Alpha 3 also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Aluminium (Al) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Heterodimeric Complex of Human RGS10 and Activated Gi Alpha 3 (pdb code 2ihb). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Heterodimeric Complex of Human RGS10 and Activated Gi Alpha 3, PDB code: 2ihb:

Magnesium binding site 1 out of 1 in 2ihb

Go back to Magnesium Binding Sites List in 2ihb
Magnesium binding site 1 out of 1 in the Crystal Structure of the Heterodimeric Complex of Human RGS10 and Activated Gi Alpha 3


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Heterodimeric Complex of Human RGS10 and Activated Gi Alpha 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg355

b:45.9
occ:1.00
O A:HOH359 1.9 44.7 1.0
O A:HOH360 1.9 41.4 1.0
OG1 A:THR181 2.0 52.6 1.0
F1 A:ALF354 2.0 52.1 1.0
O1B A:GDP356 2.1 34.9 1.0
OG A:SER47 2.2 56.0 1.0
F3 A:ALF354 2.8 53.1 1.0
CB A:THR181 3.1 52.9 1.0
CB A:SER47 3.2 55.8 1.0
PB A:GDP356 3.2 37.9 1.0
AL A:ALF354 3.2 51.0 1.0
O2B A:GDP356 3.3 34.5 1.0
N A:SER47 3.9 55.6 1.0
O A:HOH361 3.9 54.3 1.0
N A:THR181 4.0 53.2 1.0
O1A A:GDP356 4.0 40.2 1.0
CA A:SER47 4.1 55.6 1.0
CG2 A:THR181 4.1 52.2 1.0
CA A:THR181 4.1 53.1 1.0
O3B A:GDP356 4.2 37.6 1.0
OD2 A:ASP200 4.2 62.9 1.0
OD1 A:ASP200 4.3 62.5 1.0
O3A A:GDP356 4.3 38.9 1.0
O A:HOH358 4.3 42.0 1.0
F4 A:ALF354 4.4 51.2 1.0
O A:VAL201 4.4 58.4 1.0
PA A:GDP356 4.5 38.7 1.0
O2A A:GDP356 4.5 37.2 1.0
NZ A:LYS46 4.5 55.7 1.0
O A:VAL179 4.6 53.5 1.0
CG A:ASP200 4.7 61.9 1.0
CB A:LYS46 4.8 55.9 1.0
F2 A:ALF354 4.8 48.5 1.0
NH1 A:ARG178 4.9 61.6 1.0
C A:LYS46 5.0 55.7 1.0

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.
ISSN: ISSN 0027-8424
PubMed: 18434541
DOI: 10.1073/PNAS.0801508105
Page generated: Mon Dec 14 07:27:16 2020

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