Aluminium in PDB 3ab3: Crystal Structure of P115RHOGEF Rgs Domain in Complex with G Alpha 13

The structure of Crystal Structure of P115RHOGEF Rgs Domain in Complex with G Alpha 13, PDB code: 3ab3 was solved by M.Kukimoto-Niino, C.Mishima, M.Shirouzu, T.Kozasa, S.Yokoyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.88 / 2.40
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	50.481, 70.640, 88.078, 77.77, 84.45, 80.11
R / Rfree (%)	20.5 / 28

The structure of Crystal Structure of P115RHOGEF Rgs Domain in Complex with G Alpha 13 also contains other interesting chemical elements:

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

The binding sites of Aluminium atom in the Crystal Structure of P115RHOGEF Rgs Domain in Complex with G Alpha 13 (pdb code 3ab3). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Crystal Structure of P115RHOGEF Rgs Domain in Complex with G Alpha 13, PDB code: 3ab3:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in the Crystal Structure of P115RHOGEF Rgs Domain in Complex with G Alpha 13


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 P115RHOGEF Rgs Domain in Complex with G Alpha 13 within 5.0Å range: probe atom residue distance (Å) B Occ A:Al601 b:42.7 occ:1.00 AL A:ALF601 0.0 42.7 1.0 F2 A:ALF601 1.7 51.8 1.0 F1 A:ALF601 1.8 45.5 1.0 F3 A:ALF601 1.8 41.6 1.0 F4 A:ALF601 1.8 33.3 1.0 O1B A:GDP401 2.6 40.3 1.0 OE1 A:GLN226 3.6 36.9 1.0 MG A:MG501 3.7 30.3 1.0 N A:GLY225 3.7 21.8 1.0 PB A:GDP401 3.7 25.1 1.0 N A:THR203 3.9 32.4 1.0 NZ A:LYS61 4.0 37.5 1.0 NE2 A:GLN226 4.1 28.9 1.0 N A:GLU58 4.1 25.7 1.0 O3B A:GDP401 4.1 35.2 1.0 NH2 A:ARG200 4.2 30.5 1.0 CA A:GLY224 4.2 27.1 1.0 NH1 A:ARG200 4.2 32.9 1.0 O A:HOH408 4.3 19.6 1.0 CD A:GLN226 4.3 29.8 1.0 O A:THR203 4.3 31.4 1.0 CA A:GLY57 4.3 27.4 1.0 CB A:THR203 4.4 25.8 1.0 O2B A:GDP401 4.4 31.8 1.0 CE A:LYS61 4.5 30.5 1.0 C A:GLY224 4.5 25.9 1.0 O A:HOH409 4.5 48.8 1.0 CA A:GLY225 4.5 22.3 1.0 CA A:THR203 4.6 29.9 1.0 CZ A:ARG200 4.7 30.2 1.0 O A:VAL223 4.8 32.5 1.0 C A:GLY57 4.8 25.8 1.0 OG1 A:THR203 4.8 35.7 1.0 CA A:PRO202 4.8 34.4 1.0 C A:PRO202 4.9 33.0 1.0 C A:THR203 4.9 31.2 1.0 O3A A:GDP401 4.9 24.2 1.0

Aluminium binding site 2 out of 2 in the Crystal Structure of P115RHOGEF Rgs Domain in Complex with G Alpha 13


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Crystal Structure of P115RHOGEF Rgs Domain in Complex with G Alpha 13 within 5.0Å range: probe atom residue distance (Å) B Occ C:Al602 b:47.4 occ:1.00 AL C:ALF602 0.0 47.4 1.0 F2 C:ALF602 1.7 61.2 1.0 F1 C:ALF602 1.8 48.6 1.0 F3 C:ALF602 1.8 47.7 1.0 F4 C:ALF602 1.8 49.5 1.0 O1B C:GDP402 2.7 38.2 1.0 OE1 C:GLN226 3.6 37.2 1.0 PB C:GDP402 3.7 28.9 1.0 MG C:MG502 3.7 34.9 1.0 N C:THR203 3.8 37.8 1.0 N C:GLY225 3.8 25.0 1.0 NH1 C:ARG200 3.9 25.9 1.0 NE2 C:GLN226 3.9 30.6 1.0 O3B C:GDP402 4.0 37.6 1.0 NH2 C:ARG200 4.1 27.5 1.0 N C:GLU58 4.1 32.6 1.0 O C:THR203 4.1 44.7 1.0 CA C:GLY57 4.1 29.1 1.0 CA C:GLY224 4.2 35.7 1.0 NZ C:LYS61 4.2 28.3 1.0 CD C:GLN226 4.2 36.9 1.0 O C:HOH1 4.2 27.9 1.0 CB C:THR203 4.3 31.4 1.0 O C:HOH388 4.3 30.0 1.0 O2B C:GDP402 4.5 31.3 1.0 CZ C:ARG200 4.5 34.4 1.0 CA C:THR203 4.5 40.4 1.0 C C:GLY224 4.5 28.4 1.0 CA C:PRO202 4.6 37.0 1.0 CE C:LYS61 4.6 22.4 1.0 C C:GLY57 4.7 34.4 1.0 C C:PRO202 4.8 39.1 1.0 C C:THR203 4.8 42.0 1.0 O C:VAL223 4.8 41.3 1.0 CA C:GLY225 4.8 24.2 1.0 O3A C:GDP402 5.0 35.2 1.0

N.Hajicek, M.Kukimoto-Niino, C.Mishima-Tsumagari, C.R.Chow, M.Shirouzu, T.Terada, M.Patel, S.Yokoyama, T.Kozasa. Identification of Critical Residues in G(Alpha)13 For Stimulation of P115RHOGEF Activity and the Structure of the G(Alpha)13-P115RHOGEF Regulator of G Protein Signaling Homology (Rh) Domain Complex. J.Biol.Chem. V. 286 20625 2011.
ISSN: ISSN 0021-9258
PubMed: 21507947
DOI: 10.1074/JBC.M110.201392