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Magnesium in PDB 4ekd: Structure of Human Regulator of G Protein Signaling 2 (RGS2) in Complex with Murine Galpha-Q(R183C)

Enzymatic activity of Structure of Human Regulator of G Protein Signaling 2 (RGS2) in Complex with Murine Galpha-Q(R183C)

All present enzymatic activity of Structure of Human Regulator of G Protein Signaling 2 (RGS2) in Complex with Murine Galpha-Q(R183C):
3.6.5.1;

Protein crystallography data

The structure of Structure of Human Regulator of G Protein Signaling 2 (RGS2) in Complex with Murine Galpha-Q(R183C), PDB code: 4ekd was solved by J.J.G.Tesmer, M.R.Nance, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.98 / 2.71
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 60.248, 60.248, 345.569, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 25.2

Other elements in 4ekd:

The structure of Structure of Human Regulator of G Protein Signaling 2 (RGS2) in Complex with Murine Galpha-Q(R183C) also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Cobalt (Co) 2 atoms
Aluminium (Al) 1 atom
Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Human Regulator of G Protein Signaling 2 (RGS2) in Complex with Murine Galpha-Q(R183C) (pdb code 4ekd). 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 Structure of Human Regulator of G Protein Signaling 2 (RGS2) in Complex with Murine Galpha-Q(R183C), PDB code: 4ekd:

Magnesium binding site 1 out of 1 in 4ekd

Go back to Magnesium Binding Sites List in 4ekd
Magnesium binding site 1 out of 1 in the Structure of Human Regulator of G Protein Signaling 2 (RGS2) in Complex with Murine Galpha-Q(R183C)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Regulator of G Protein Signaling 2 (RGS2) in Complex with Murine Galpha-Q(R183C) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg407

b:60.9
occ:1.00
 F3 A:ALF402 1.7 62.5 1.0
O A:HOH502 1.8 64.7 1.0
O A:HOH503 1.8 63.3 1.0
OG A:SER53 2.1 78.5 1.0
O2B A:GDP401 2.1 63.7 1.0
OG1 A:THR186 2.2 77.9 1.0
O3B A:GDP401 3.0 63.0 1.0
PB A:GDP401 3.0 63.5 1.0
CB A:THR186 3.1 78.7 1.0
CB A:SER53 3.1 79.6 1.0
AL A:ALF402 3.3 62.0 1.0
F1 A:ALF402 3.5 64.5 1.0
N A:SER53 3.6 78.5 1.0
N A:THR186 3.7 81.7 1.0
O2A A:GDP401 3.8 66.6 1.0
CA A:SER53 3.9 80.5 1.0
CA A:THR186 4.0 81.4 1.0
O1B A:GDP401 4.0 62.6 1.0
OD2 A:ASP205 4.0 91.6 1.0
F2 A:ALF402 4.1 63.0 1.0
O3A A:GDP401 4.1 64.8 1.0
OD1 A:ASP205 4.1 88.8 1.0
PA A:GDP401 4.2 67.0 1.0
CG2 A:THR186 4.2 78.1 1.0
O1A A:GDP401 4.3 68.4 1.0
O A:HOH501 4.4 63.8 1.0
O A:VAL184 4.4 84.8 1.0
CG A:ASP205 4.5 90.6 1.0
O A:VAL206 4.5 77.9 1.0
CB A:LYS52 4.7 74.1 1.0
C A:PRO185 4.7 85.8 1.0
C A:LYS52 4.7 78.9 1.0
NZ A:LYS52 4.9 71.1 1.0
N A:LYS52 5.0 74.7 1.0

Reference:

M.R.Nance, B.Kreutz, V.M.Tesmer, R.Sterne-Marr, T.Kozasa, J.J.Tesmer. Structural and Functional Analysis of the Regulator of G Protein Signaling 2-G Alpha Q Complex. Structure V. 21 438 2013.
ISSN: ISSN 0969-2126
PubMed: 23434405
DOI: 10.1016/J.STR.2012.12.016
Page generated: Fri Aug 16 14:31:05 2024

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