Magnesium in PDB 4arz: The Crystal Structure of GTR1P-GTR2P Complexed with Gtp-Gdp

The structure of The Crystal Structure of GTR1P-GTR2P Complexed with Gtp-Gdp, PDB code: 4arz was solved by J.H.Jeong, Y.G.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30 / 3.10
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	90.712, 148.897, 117.759, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 27.19

The binding sites of Magnesium atom in the The Crystal Structure of GTR1P-GTR2P Complexed with Gtp-Gdp (pdb code 4arz). 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 The Crystal Structure of GTR1P-GTR2P Complexed with Gtp-Gdp, PDB code: 4arz:

Magnesium binding site 1 out of 1 in the The Crystal Structure of GTR1P-GTR2P Complexed with Gtp-Gdp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of GTR1P-GTR2P Complexed with Gtp-Gdp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg500 b:38.3 occ:1.00 OG A:SER20 2.2 70.1 1.0 OG1 A:THR41 2.2 83.8 1.0 O1B A:GTP400 2.4 81.5 1.0 PG A:GTP400 2.7 92.1 1.0 O1G A:GTP400 2.7 92.3 1.0 CB A:SER20 2.9 69.2 1.0 PB A:GTP400 3.1 80.9 1.0 O3B A:GTP400 3.2 86.5 1.0 O1A A:GTP400 3.3 81.9 1.0 O3A A:GTP400 3.4 80.4 1.0 N A:THR41 3.5 86.1 1.0 CB A:THR41 3.5 84.4 1.0 O2G A:GTP400 3.7 92.2 1.0 PA A:GTP400 3.9 79.4 1.0 O3G A:GTP400 4.1 91.7 1.0 CG2 A:THR41 4.1 83.7 1.0 CA A:THR41 4.1 85.0 1.0 CA A:SER20 4.1 68.2 1.0 N A:SER20 4.2 68.4 1.0 O A:GLY39 4.4 88.8 1.0 C A:ALA40 4.5 87.4 1.0 O2B A:GTP400 4.5 83.7 1.0 OD1 A:ASP61 4.6 86.0 1.0 O2A A:GTP400 4.6 77.5 1.0 OD2 A:ASP61 4.6 86.3 1.0 CA A:ALA40 4.7 87.8 1.0 CG A:ASP61 4.9 85.5 1.0

J.H.Jeong, K.H.Lee, Y.M.Kim, D.H.Kim, B.H.Oh, Y.G.Kim. Crystal Structure of the GTR1PGTP-GTR2PGDP Complex Reveals Large Structural Rearrangements Triggered By Gtp-to-Gdp Conversion J.Biol.Chem. V. 287 29648 2012.
ISSN: ISSN 0021-9258
PubMed: 22807443
DOI: 10.1074/JBC.C112.384420