Magnesium in PDB 4euk: Crystal Structure

All present enzymatic activity of Crystal Structure:
2.7.13.3;

The structure of Crystal Structure, PDB code: 4euk was solved by T.Stehle, J.Bauer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.76 / 1.95
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	106.800, 106.800, 106.800, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 19.7

The binding sites of Magnesium atom in the Crystal Structure (pdb code 4euk). 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, PDB code: 4euk:

Magnesium binding site 1 out of 1 in the Crystal Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1001 b:29.2 occ:1.00 OD2 A:ASP828 1.9 29.2 1.0 OD1 A:ASP785 2.0 31.1 1.0 O A:CYS830 2.0 35.1 1.0 O A:HOH1171 2.1 32.1 1.0 O A:HOH1170 2.1 25.9 1.0 O A:HOH1169 2.1 32.1 1.0 CG A:ASP828 3.0 26.6 1.0 CG A:ASP785 3.1 35.8 1.0 C A:CYS830 3.3 34.6 1.0 OD1 A:ASP828 3.3 33.0 1.0 OD2 A:ASP785 3.4 40.4 1.0 OE2 A:GLU784 3.7 31.1 1.0 CG A:MET831 4.1 29.4 1.0 NZ A:LYS906 4.1 27.4 1.0 CA A:CYS830 4.1 34.8 0.5 CA A:CYS830 4.1 33.6 0.5 N A:MET831 4.2 32.7 1.0 CB A:ASP828 4.3 22.4 1.0 CB A:CYS830 4.3 38.4 0.5 N A:CYS830 4.3 34.3 1.0 O A:HOH1104 4.3 29.5 1.0 CB A:CYS830 4.3 37.2 0.5 CA A:MET831 4.4 33.9 1.0 CB A:ASP785 4.4 32.1 1.0 O A:HOH1172 4.5 34.1 1.0 N A:ASP785 4.5 26.8 1.0 CD A:GLU784 4.6 31.2 1.0 NE2 B:HIS79 4.6 61.8 1.0 CB A:MET831 4.8 30.5 1.0 OE1 A:GLU784 4.9 30.1 1.0 O B:HOH367 4.9 52.5 1.0 CA A:ASP785 5.0 31.7 1.0

J.Bauer, K.Reiss, M.Veerabagu, M.Heunemann, K.Harter, T.Stehle. Structure-Function Analysis of Arabidopsis Thaliana Histidine Kinase AHK5 Bound to Its Cognate Phosphotransfer Protein AHP1. Mol Plant V. 6 959 2013.
ISSN: ISSN 1674-2052
PubMed: 23132142
DOI: 10.1093/MP/SSS126