Aluminium in PDB 3c7k: Molecular Architecture of Galphao and the Structural Basis For RGS16- Mediated Deactivation

The structure of Molecular Architecture of Galphao and the Structural Basis For RGS16- Mediated Deactivation, PDB code: 3c7k was solved by K.C.Slep, M.A.Kercher, T.Wieland, C.Chen, M.I.Simon, P.B.Sigler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.90
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	96.357, 96.357, 235.610, 90.00, 90.00, 120.00
R / Rfree (%)	25 / 31.1

The structure of Molecular Architecture of Galphao and the Structural Basis For RGS16- Mediated Deactivation also contains other interesting chemical elements:

Fluorine	(F)	8 atoms
Magnesium	(Mg)	2 atoms

The binding sites of Aluminium atom in the Molecular Architecture of Galphao and the Structural Basis For RGS16- Mediated Deactivation (pdb code 3c7k). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Molecular Architecture of Galphao and the Structural Basis For RGS16- Mediated Deactivation, PDB code: 3c7k:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in the Molecular Architecture of Galphao and the Structural Basis For RGS16- Mediated Deactivation


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Molecular Architecture of Galphao and the Structural Basis For RGS16- Mediated Deactivation within 5.0Å range: probe atom residue distance (Å) B Occ A:Al365 b:15.8 occ:1.00 AL A:ALF365 0.0 15.8 1.0 F1 A:ALF365 1.8 15.6 1.0 F3 A:ALF365 1.8 15.5 1.0 F2 A:ALF365 1.8 16.8 1.0 F4 A:ALF365 1.8 16.9 1.0 O A:HOH401 2.1 0.3 1.0 O3B A:GDP361 2.5 14.5 1.0 PB A:GDP361 3.1 15.1 1.0 O2B A:GDP361 3.2 14.0 1.0 MG A:MG362 3.3 18.9 1.0 O1B A:GDP361 3.5 15.3 1.0 NH1 A:ARG179 3.6 64.6 1.0 NZ A:LYS46 3.7 69.8 1.0 N A:GLU43 3.9 75.8 1.0 NE2 A:GLN205 4.0 63.9 1.0 NH2 A:ARG179 4.0 67.1 1.0 N A:GLY204 4.1 80.3 1.0 N A:THR182 4.1 68.8 1.0 CZ A:ARG179 4.3 65.0 1.0 OE1 A:GLN205 4.3 63.2 1.0 CE A:LYS46 4.3 71.4 1.0 O3A A:GDP361 4.4 16.9 1.0 CD A:GLN205 4.6 63.4 1.0 O A:HOH403 4.6 79.8 1.0 CA A:GLU43 4.6 76.0 1.0 CA A:LYS181 4.6 68.2 1.0 CA A:GLY42 4.6 74.2 1.0 CB A:THR182 4.6 70.0 1.0 CG A:LYS181 4.7 70.1 1.0 CA A:GLY204 4.7 77.4 1.0 OG1 A:THR182 4.7 68.7 1.0 O A:THR182 4.7 71.6 1.0 C A:GLY42 4.7 75.3 1.0 O A:HOH402 4.8 78.7 1.0 O A:VAL202 4.8 89.3 1.0 C A:LYS181 4.9 67.9 1.0 CA A:THR182 4.9 70.3 1.0 CA A:GLY203 5.0 84.7 1.0 O2A A:GDP361 5.0 13.4 1.0

Aluminium binding site 2 out of 2 in the Molecular Architecture of Galphao and the Structural Basis For RGS16- Mediated Deactivation


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Molecular Architecture of Galphao and the Structural Basis For RGS16- Mediated Deactivation within 5.0Å range: probe atom residue distance (Å) B Occ C:Al365 b:57.9 occ:1.00 AL C:ALF365 0.0 57.9 1.0 F4 C:ALF365 1.7 60.9 1.0 F1 C:ALF365 1.7 57.7 1.0 F2 C:ALF365 1.8 58.8 1.0 F3 C:ALF365 1.8 49.9 1.0 O C:HOH401 2.3 0.3 1.0 O3B C:GDP361 2.6 14.5 1.0 PB C:GDP361 3.6 15.1 1.0 O2B C:GDP361 3.6 14.0 1.0 NZ C:LYS46 3.6 70.7 1.0 NH1 C:ARG179 3.6 66.2 1.0 MG C:MG362 3.7 71.2 1.0 N C:THR182 4.0 75.9 1.0 N C:GLU43 4.0 76.2 1.0 OE1 C:GLN205 4.1 68.5 1.0 N C:GLY204 4.1 79.0 1.0 NH2 C:ARG179 4.1 64.8 1.0 O1B C:GDP361 4.2 15.3 1.0 CZ C:ARG179 4.3 65.4 1.0 O C:HOH402 4.4 78.7 1.0 CB C:THR182 4.4 77.2 1.0 O C:THR182 4.5 80.3 1.0 CE C:LYS46 4.5 72.3 1.0 NE2 C:GLN205 4.5 70.8 1.0 O C:HOH403 4.6 79.8 1.0 CA C:LYS181 4.6 75.9 1.0 CG C:LYS181 4.6 77.5 1.0 CA C:GLU43 4.6 76.5 1.0 CA C:THR182 4.7 77.8 1.0 O3A C:GDP361 4.7 16.9 1.0 CD C:GLN205 4.7 68.8 1.0 CA C:GLY204 4.8 76.5 1.0 C C:LYS181 4.8 75.7 1.0 CA C:GLY42 4.8 74.3 1.0 C C:GLY42 4.8 75.3 1.0 OG1 C:THR182 4.9 76.9 1.0 O C:VAL202 4.9 90.0 1.0 O2A C:GDP361 5.0 13.4 1.0

K.C.Slep, M.A.Kercher, T.Wieland, C.K.Chen, M.I.Simon, P.B.Sigler. Molecular Architecture of G{Alpha}O and the Structural Basis For RGS16-Mediated Deactivation. Proc.Natl.Acad.Sci.Usa V. 105 6243 2008.
ISSN: ISSN 0027-8424
PubMed: 18434540
DOI: 10.1073/PNAS.0801569105