Magnesium in PDB 2hxs: Crystal Structure of RAB28A Gtpase in the Inactive (Gdp-3'P- Bound) Form

The structure of Crystal Structure of RAB28A Gtpase in the Inactive (Gdp-3'P- Bound) Form, PDB code: 2hxs was solved by S.H.Lee, Y.Li, R.Dominguez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.00 / 1.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	30.510, 56.621, 85.109, 90.00, 90.00, 90.00
R / Rfree (%)	14.9 / 18.4

The binding sites of Magnesium atom in the Crystal Structure of RAB28A Gtpase in the Inactive (Gdp-3'P- Bound) Form (pdb code 2hxs). 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 Crystal Structure of RAB28A Gtpase in the Inactive (Gdp-3'P- Bound) Form, PDB code: 2hxs:

Magnesium binding site 1 out of 1 in the Crystal Structure of RAB28A Gtpase in the Inactive (Gdp-3'P- Bound) Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of RAB28A Gtpase in the Inactive (Gdp-3'P- Bound) Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:12.6 occ:1.00 O2B A:G3D401 2.0 11.7 1.0 O A:HOH484 2.1 15.2 1.0 O A:HOH603 2.1 14.5 1.0 O A:HOH582 2.1 14.9 1.0 OG1 A:THR26 2.1 12.0 1.0 O A:HOH516 2.1 12.6 1.0 CB A:THR26 3.2 12.1 1.0 PB A:G3D401 3.2 11.9 1.0 O3B A:G3D401 3.5 13.5 1.0 N A:THR26 3.9 11.1 1.0 O A:GLY70 4.1 14.0 1.0 CA A:THR26 4.1 11.1 1.0 O A:HOH424 4.2 19.2 1.0 O2A A:G3D401 4.2 13.8 1.0 CG2 A:THR26 4.2 13.3 1.0 OD2 A:ASP68 4.2 14.7 1.0 OD1 A:ASP68 4.3 14.4 1.0 O1B A:G3D401 4.3 11.7 1.0 O3A A:G3D401 4.3 12.4 1.0 O A:HOH543 4.4 29.4 1.0 C A:GLY70 4.5 12.9 1.0 CA A:GLY70 4.5 13.5 1.0 PA A:G3D401 4.6 12.1 1.0 CG A:ASP68 4.7 13.6 1.0 O1A A:G3D401 4.8 13.0 1.0 CB A:LYS25 4.9 11.5 1.0 NZ A:LYS25 4.9 12.6 1.0 O A:HOH409 4.9 15.4 1.0 O A:HOH546 4.9 38.2 1.0 C A:LYS25 5.0 10.7 1.0

S.H.Lee, Y.Li, R.Dominguez. The Crystal Structure of RAB28 Gtpase in Active and Inactive Forms To Be Published.