Magnesium in PDB 3e5h: Crystal Structure of RAB28 Gtpase in the Active (Gppnhp-Bound) Form

The structure of Crystal Structure of RAB28 Gtpase in the Active (Gppnhp-Bound) Form, PDB code: 3e5h was solved by S.H.Lee, K.Baek, Y.Li, R.Dominguez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.79 / 1.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	79.747, 79.747, 66.977, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / 18.1

The binding sites of Magnesium atom in the Crystal Structure of RAB28 Gtpase in the Active (Gppnhp-Bound) Form (pdb code 3e5h). 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 RAB28 Gtpase in the Active (Gppnhp-Bound) Form, PDB code: 3e5h:

Magnesium binding site 1 out of 1 in the Crystal Structure of RAB28 Gtpase in the Active (Gppnhp-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 RAB28 Gtpase in the Active (Gppnhp-Bound) Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg200 b:14.4 occ:1.00 O2G A:GNP201 2.0 14.9 1.0 OG1 A:THR26 2.1 14.3 1.0 O2B A:GNP201 2.1 12.9 1.0 O A:HOH375 2.1 14.9 1.0 OG1 A:THR44 2.1 15.1 1.0 O A:HOH333 2.1 15.8 1.0 CB A:THR44 3.1 15.2 1.0 CB A:THR26 3.1 14.8 1.0 PG A:GNP201 3.2 13.9 1.0 PB A:GNP201 3.3 12.6 1.0 N3B A:GNP201 3.4 12.4 1.0 N A:THR44 3.7 16.1 1.0 O3G A:GNP201 3.8 16.6 1.0 N A:THR26 3.9 13.0 1.0 CA A:THR44 4.0 15.8 1.0 OD2 A:ASP68 4.1 18.8 1.0 CA A:THR26 4.1 13.3 1.0 OD1 A:ASP68 4.1 18.1 1.0 O2A A:GNP201 4.2 14.3 1.0 CG2 A:THR26 4.2 16.1 1.0 CG2 A:THR44 4.2 16.9 1.0 O3A A:GNP201 4.3 13.0 1.0 O A:HOH218 4.3 22.8 1.0 O1B A:GNP201 4.4 13.2 1.0 O1G A:GNP201 4.4 16.7 1.0 CG A:ASP68 4.5 16.9 1.0 O A:LYS42 4.5 18.8 1.0 PA A:GNP201 4.6 14.0 1.0 O1A A:GNP201 4.7 14.4 1.0 C A:GLN43 4.8 16.9 1.0

S.H.Lee, K.Baek, R.Dominguez. Large Nucleotide-Dependent Conformational Change in RAB28. Febs Lett. V. 582 4107 2008.
ISSN: ISSN 0014-5793
PubMed: 19026641
DOI: 10.1016/J.FEBSLET.2008.11.008