Magnesium in PDB 3uzt: Structure of the C13.18 Rna Aptamer in Complex with G Protein-Coupled Receptor Kinase 2

All present enzymatic activity of Structure of the C13.18 Rna Aptamer in Complex with G Protein-Coupled Receptor Kinase 2:
2.7.11.15;

The structure of Structure of the C13.18 Rna Aptamer in Complex with G Protein-Coupled Receptor Kinase 2, PDB code: 3uzt was solved by J.J.G.Tesmer, V.M.Tesmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.88 / 3.51
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	113.346, 139.719, 60.949, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 31.7

The binding sites of Magnesium atom in the Structure of the C13.18 Rna Aptamer in Complex with G Protein-Coupled Receptor Kinase 2 (pdb code 3uzt). 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 the C13.18 Rna Aptamer in Complex with G Protein-Coupled Receptor Kinase 2, PDB code: 3uzt:

Magnesium binding site 1 out of 1 in the Structure of the C13.18 Rna Aptamer in Complex with G Protein-Coupled Receptor Kinase 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the C13.18 Rna Aptamer in Complex with G Protein-Coupled Receptor Kinase 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg690 b:92.6 occ:1.00 OD2 A:ASP335 1.9 0.2 1.0 OP1 B:U50 2.0 1.0 1.0 CG A:ASP335 2.9 0.3 1.0 OD1 A:ASP335 3.2 0.5 1.0 P B:U50 3.3 0.3 1.0 C5' B:U50 3.8 0.3 1.0 OP2 B:U50 3.9 0.9 1.0 O5' B:U50 3.9 0.1 1.0 CB A:ASP335 4.2 0.5 1.0 OP1 B:A51 4.2 0.5 1.0 O3' B:A49 4.5 0.2 1.0 C4' B:U50 4.8 0.5 1.0 NZ A:LYS220 4.8 0.1 1.0 CA A:GLY337 4.8 0.8 1.0 CE A:LYS220 5.0 0.8 1.0

V.M.Tesmer, S.Lennarz, G.Mayer, J.J.Tesmer. Molecular Mechanism For Inhibition of G Protein-Coupled Receptor Kinase 2 By A Selective Rna Aptamer. Structure V. 20 1300 2012.
ISSN: ISSN 0969-2126
PubMed: 22727813
DOI: 10.1016/J.STR.2012.05.002