Magnesium in PDB 5szh: Structure of Human RAB1B in Complex with the Bmerb Domain of Mical-Cl

The structure of Structure of Human RAB1B in Complex with the Bmerb Domain of Mical-Cl, PDB code: 5szh was solved by A.Rai, A.Oprisko, J.Campos, Y.Fu, T.Friese, R.S.Goody, M.P.Mueller, E.M.Gazdag, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.83 / 2.30
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	61.750, 129.380, 129.850, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 20.7

The binding sites of Magnesium atom in the Structure of Human RAB1B in Complex with the Bmerb Domain of Mical-Cl (pdb code 5szh). 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 Human RAB1B in Complex with the Bmerb Domain of Mical-Cl, PDB code: 5szh:

Magnesium binding site 1 out of 1 in the Structure of Human RAB1B in Complex with the Bmerb Domain of Mical-Cl


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human RAB1B in Complex with the Bmerb Domain of Mical-Cl within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:49.8 occ:1.00 O1G B:GNP301 2.0 72.7 1.0 OG B:SER22 2.0 57.4 1.0 O1B B:GNP301 2.0 53.2 1.0 O B:HOH404 2.1 49.7 1.0 O B:HOH410 2.1 48.6 1.0 OG1 B:THR40 2.1 57.5 1.0 CB B:SER22 3.1 44.9 1.0 PG B:GNP301 3.2 54.5 1.0 CB B:THR40 3.2 56.8 1.0 PB B:GNP301 3.3 52.9 1.0 N3B B:GNP301 3.5 0.3 1.0 N B:THR40 3.8 57.5 1.0 N B:SER22 3.8 47.6 1.0 O2G B:GNP301 3.8 43.8 1.0 OD2 B:ASP63 3.8 76.7 1.0 CA B:SER22 4.0 51.6 1.0 O2A B:GNP301 4.0 53.4 1.0 CA B:THR40 4.1 55.9 1.0 OD1 B:ASP63 4.2 78.3 1.0 O2B B:GNP301 4.3 73.2 1.0 O3G B:GNP301 4.3 65.6 1.0 O3A B:GNP301 4.3 84.1 1.0 CG2 B:THR40 4.4 60.9 1.0 CG B:ASP63 4.4 76.3 1.0 PA B:GNP301 4.5 56.7 1.0 O B:THR64 4.6 50.5 1.0 O1A B:GNP301 4.6 75.2 1.0 O B:ILE38 4.7 61.6 1.0 C B:SER39 4.8 62.8 1.0 CB B:LYS21 4.8 40.0 1.0 C B:LYS21 4.9 53.4 1.0

A.Rai, A.Oprisko, J.Campos, Y.Fu, T.Friese, A.Itzen, R.S.Goody, E.M.Gazdag, M.P.Muller. Bmerb Domains Are Bivalent RAB8 Family Effectors Evolved By Gene Duplication. Elife V. 5 2016.
ISSN: ESSN 2050-084X
PubMed: 27552051
DOI: 10.7554/ELIFE.18675