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

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

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
Magnesium	(Mg)	1 atom

The binding sites of Aluminium 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 Aluminium atom.
In total only one binding site of Aluminium was determined in the Crystal Structure of the Heterodimeric Complex of Human RGS10 and Activated Gi Alpha 3, PDB code: 2ihb:

Aluminium 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 Aluminium with other atoms in the Al 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:Al354 b:51.0 occ:1.00 AL A:ALF354 0.0 51.0 1.0 F3 A:ALF354 1.8 53.1 1.0 F1 A:ALF354 1.8 52.1 1.0 F4 A:ALF354 1.8 51.2 1.0 F2 A:ALF354 1.8 48.5 1.0 O2B A:GDP356 2.0 34.5 1.0 O A:HOH358 2.0 42.0 1.0 MG A:MG355 3.2 45.9 1.0 PB A:GDP356 3.3 37.9 1.0 NZ A:LYS46 3.6 55.7 1.0 O1B A:GDP356 3.6 34.9 1.0 O A:HOH360 3.8 41.4 1.0 NH1 A:ARG178 3.8 61.6 1.0 N A:THR181 3.9 53.2 1.0 N A:GLU43 3.9 57.4 1.0 OE1 A:GLN204 4.0 53.2 1.0 O3B A:GDP356 4.0 37.6 1.0 OG1 A:THR181 4.0 52.6 1.0 N A:GLY203 4.1 56.5 1.0 NE2 A:GLN204 4.2 51.6 1.0 O A:HOH359 4.2 44.7 1.0 CA A:GLY42 4.2 56.4 1.0 CB A:THR181 4.3 52.9 1.0 NH2 A:ARG178 4.3 60.4 1.0 O3A A:GDP356 4.4 38.9 1.0 O A:THR181 4.5 53.4 1.0 CD A:GLN204 4.5 53.1 1.0 CA A:GLY202 4.5 57.3 1.0 CZ A:ARG178 4.5 60.6 1.0 C A:GLY42 4.6 56.6 1.0 CA A:THR181 4.6 53.1 1.0 CA A:LYS180 4.8 54.1 1.0 O A:VAL201 4.8 58.4 1.0 C A:GLY202 4.8 56.9 1.0 C A:LYS180 4.9 53.3 1.0 CA A:GLU43 4.9 58.2 1.0 CA A:GLY203 4.9 56.1 1.0 CG A:LYS180 5.0 56.4 1.0 CE A:LYS46 5.0 56.6 1.0 O1A A:GDP356 5.0 40.2 1.0

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