Aluminium in PDB 4ekc: 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;

The structure of Structure of Human Regulator of G Protein Signaling 2 (RGS2) in Complex with Murine Galpha-Q(R183C), PDB code: 4ekc 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)	19.98 / 7.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	139.603, 124.983, 97.196, 90.00, 124.13, 90.00
R / Rfree (%)	15.8 / 22

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)	8 atoms
Magnesium	(Mg)	2 atoms

The binding sites of Aluminium atom in the Structure of Human Regulator of G Protein Signaling 2 (RGS2) in Complex with Murine Galpha-Q(R183C) (pdb code 4ekc). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Structure of Human Regulator of G Protein Signaling 2 (RGS2) in Complex with Murine Galpha-Q(R183C), PDB code: 4ekc:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 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 Aluminium with other atoms in the Al 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:Al401 b:43.5 occ:1.00 AL A:ALF401 0.0 43.5 1.0 O A:HOH501 1.8 43.7 1.0 F2 A:ALF401 1.8 46.6 1.0 F1 A:ALF401 1.8 44.6 1.0 F3 A:ALF401 1.8 45.4 1.0 F4 A:ALF401 1.8 44.3 1.0 O3B A:GDP400 2.2 61.4 1.0 PB A:GDP400 2.8 62.7 1.0 O2B A:GDP400 3.0 63.4 1.0 O1B A:GDP400 3.3 62.3 1.0 MG A:MG402 3.3 69.1 1.0 O A:HOH502 3.7 75.2 1.0 NZ A:LYS52 3.9 74.2 1.0 N A:GLY208 3.9 0.7 1.0 O A:HOH503 4.0 0.5 1.0 OE1 A:GLN209 4.0 0.5 1.0 N A:GLU49 4.1 67.1 1.0 NE2 A:GLN209 4.2 0.1 1.0 O3A A:GDP400 4.3 68.5 1.0 N A:THR186 4.4 0.3 1.0 CA A:GLY208 4.5 0.2 1.0 CD A:GLN209 4.6 0.2 1.0 CG A:GLU49 4.6 72.3 1.0 O2A A:GDP400 4.6 74.6 1.0 CE A:LYS52 4.6 75.3 1.0 CA A:GLU49 4.6 68.1 1.0 O A:VAL206 4.8 0.8 1.0 O A:THR186 4.8 0.9 1.0 CA A:GLY207 4.9 0.1 1.0 C A:GLY207 4.9 0.7 1.0 OG1 A:THR186 4.9 0.8 1.0 CA A:GLY48 5.0 67.7 1.0

Aluminium binding site 2 out of 2 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 Aluminium with other atoms in the Al binding site number 2 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 C:Al401 b:60.2 occ:1.00 AL C:ALF401 0.0 60.2 1.0 O C:HOH501 1.8 65.9 1.0 F2 C:ALF401 1.8 61.9 1.0 F1 C:ALF401 1.8 61.5 1.0 F3 C:ALF401 1.8 60.5 1.0 F4 C:ALF401 1.8 61.0 1.0 O3B C:GDP400 2.2 60.4 1.0 PB C:GDP400 2.8 59.4 1.0 O2B C:GDP400 3.0 59.7 1.0 O1B C:GDP400 3.3 59.8 1.0 MG C:MG402 3.3 64.5 1.0 O C:HOH502 3.7 80.2 1.0 NZ C:LYS52 3.8 77.5 1.0 N C:GLY208 3.9 0.7 1.0 O C:HOH503 4.0 75.5 1.0 OE1 C:GLN209 4.1 0.6 1.0 N C:GLU49 4.1 87.1 1.0 NE2 C:GLN209 4.2 0.6 1.0 O3A C:GDP400 4.3 61.1 1.0 N C:THR186 4.5 0.6 1.0 CA C:GLY208 4.5 0.1 1.0 CD C:GLN209 4.6 0.5 1.0 CG C:GLU49 4.6 92.6 1.0 CE C:LYS52 4.6 77.9 1.0 CA C:GLU49 4.6 87.0 1.0 O2A C:GDP400 4.6 63.0 1.0 O C:VAL206 4.8 96.8 1.0 O C:THR186 4.8 0.7 1.0 CA C:GLY207 4.9 0.8 1.0 OG1 C:THR186 4.9 0.4 1.0 C C:GLY207 4.9 0.8 1.0 CB C:THR186 5.0 0.4 1.0 CA C:GLY48 5.0 89.8 1.0

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