Magnesium in PDB 5j5c: Crystal Structure of ARL1-Gtp and Dcb Domain of BIG1 Complex

The structure of Crystal Structure of ARL1-Gtp and Dcb Domain of BIG1 Complex, PDB code: 5j5c was solved by R.Wang, Z.Wang, T.Zhang, J.Ding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 3.40
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	107.819, 107.819, 204.627, 90.00, 90.00, 120.00
R / Rfree (%)	22.5 / 25.8

The binding sites of Magnesium atom in the Crystal Structure of ARL1-Gtp and Dcb Domain of BIG1 Complex (pdb code 5j5c). 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 ARL1-Gtp and Dcb Domain of BIG1 Complex, PDB code: 5j5c:

Magnesium binding site 1 out of 1 in the Crystal Structure of ARL1-Gtp and Dcb Domain of BIG1 Complex


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 ARL1-Gtp and Dcb Domain of BIG1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg201 b:76.3 occ:1.00 O1G A:GTP204 2.1 100.0 1.0 OG1 A:THR31 2.1 98.3 1.0 OG1 A:THR48 2.1 1.0 1.0 O1B A:GTP204 2.6 96.9 1.0 O1A A:GTP204 3.1 0.8 1.0 PG A:GTP204 3.2 99.2 1.0 O A:ILE46 3.2 0.6 1.0 N A:THR48 3.2 0.3 1.0 O3B A:GTP204 3.2 99.7 1.0 CB A:THR31 3.3 96.2 1.0 CB A:THR48 3.3 0.5 1.0 PB A:GTP204 3.5 95.9 1.0 CA A:THR48 3.8 0.5 1.0 O2G A:GTP204 3.8 96.1 1.0 OD2 A:ASP67 4.0 0.5 1.0 CG2 A:THR31 4.0 95.6 1.0 C A:PRO47 4.1 0.5 1.0 CA A:PRO47 4.2 0.4 1.0 PA A:GTP204 4.3 0.9 1.0 C A:ILE46 4.3 0.9 1.0 O3A A:GTP204 4.4 95.9 1.0 CA A:THR31 4.4 94.1 1.0 O3G A:GTP204 4.5 92.5 1.0 N A:THR31 4.5 91.0 1.0 CG2 A:THR48 4.5 0.6 1.0 OD1 A:ASP67 4.6 0.0 1.0 N A:PRO47 4.7 0.4 1.0 CG A:ASP67 4.7 0.2 1.0 O2B A:GTP204 4.8 92.7 1.0

R.Wang, Z.Wang, K.Wang, T.Zhang, J.Ding. Structural Basis For Targeting BIG1 to Golgi Apparatus Through Interaction of Its Dcb Domain with ARL1 J Mol Cell Biol 2016.
ISSN: ESSN 1759-4685
PubMed: 27436755
DOI: 10.1093/JMCB/MJW033