Magnesium in PDB 5c1t: Crystal Structure of the Gtp-Bound Wild Type EHRABX3 From Entamoeba Histolytica

The structure of Crystal Structure of the Gtp-Bound Wild Type EHRABX3 From Entamoeba Histolytica, PDB code: 5c1t was solved by V.K.Srivastava, M.Chandra, S.Datta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.69 / 2.80
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	62.965, 62.965, 312.021, 90.00, 90.00, 120.00
R / Rfree (%)	26.3 / 30.2

The binding sites of Magnesium atom in the Crystal Structure of the Gtp-Bound Wild Type EHRABX3 From Entamoeba Histolytica (pdb code 5c1t). 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 the Gtp-Bound Wild Type EHRABX3 From Entamoeba Histolytica, PDB code: 5c1t:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Gtp-Bound Wild Type EHRABX3 From Entamoeba Histolytica


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 the Gtp-Bound Wild Type EHRABX3 From Entamoeba Histolytica within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:79.8 occ:1.00 O3B B:GTP402 2.0 51.4 1.0 OG1 B:THR34 2.0 63.5 1.0 O2A B:GTP402 2.1 64.0 1.0 O1B B:GTP402 2.2 82.1 1.0 O1G B:GTP402 2.2 65.5 1.0 PB B:GTP402 2.5 61.5 1.0 PG B:GTP402 2.6 70.4 1.0 PA B:GTP402 3.1 63.1 1.0 O3A B:GTP402 3.2 46.6 1.0 CB B:THR34 3.3 54.2 1.0 O2G B:GTP402 3.4 71.0 1.0 CG2 B:THR34 3.7 65.0 1.0 O2B B:GTP402 3.9 64.1 1.0 O3G B:GTP402 3.9 58.8 1.0 O5' B:GTP402 4.2 62.2 1.0 O1A B:GTP402 4.2 43.0 1.0 N B:THR34 4.3 43.4 1.0 CA B:THR34 4.4 43.9 1.0 C5' B:GTP402 4.4 65.5 1.0 O B:GLY30 4.7 65.3 1.0

V.K.Srivastava, M.Chandra, Y.Saito-Nakano, T.Nozaki, S.Datta. Crystal Structure Analysis of Wild Type and Fast Hydrolyzing Mutant of EHRABX3, A Tandem Ras Superfamily Gtpase From Entamoeba Histolytica. J.Mol.Biol. V. 428 41 2016.
ISSN: ESSN 1089-8638
PubMed: 26555751
DOI: 10.1016/J.JMB.2015.11.003