Magnesium in PDB 6j2l: Crystal Structure of Bi-Functional Enzyme

All present enzymatic activity of Crystal Structure of Bi-Functional Enzyme:
3.5.4.19; 3.6.1.31;

The structure of Crystal Structure of Bi-Functional Enzyme, PDB code: 6j2l was solved by H.Zhang, G.Shang, Y.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.75 / 2.17
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	169.050, 45.230, 65.259, 90.00, 112.53, 90.00
R / Rfree (%)	20.4 / 24.9

The structure of Crystal Structure of Bi-Functional Enzyme also contains other interesting chemical elements:

Zinc

(Zn)

5 atoms

The binding sites of Magnesium atom in the Crystal Structure of Bi-Functional Enzyme (pdb code 6j2l). 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 Bi-Functional Enzyme, PDB code: 6j2l:

Magnesium binding site 1 out of 1 in the Crystal Structure of Bi-Functional Enzyme


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 Bi-Functional Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:56.1 occ:1.00 OE2 B:GLU172 2.1 73.4 1.0 CG B:GLU153 2.6 57.9 1.0 OE1 B:GLU156 2.6 72.5 1.0 OD2 B:ASP175 2.7 59.0 1.0 OE2 B:GLU153 2.9 67.8 1.0 CD B:GLU153 3.1 67.8 1.0 CD B:GLU172 3.1 58.2 1.0 CB B:ASP175 3.4 44.4 1.0 CG B:ASP175 3.5 52.6 1.0 CG B:GLU172 3.6 53.6 1.0 CD B:GLU156 3.8 72.3 1.0 CB B:GLU153 3.9 45.9 1.0 OE1 B:GLU172 4.1 82.1 1.0 OE1 B:GLU153 4.2 63.6 1.0 CA B:GLU172 4.5 44.4 1.0 CA B:GLU153 4.5 46.1 1.0 OE2 B:GLU156 4.5 71.5 1.0 CB B:GLU156 4.6 45.1 1.0 OD1 B:ASP175 4.7 48.1 1.0 CB B:GLU172 4.7 50.5 1.0 O B:GLU172 4.7 47.8 1.0 CG B:GLU156 4.8 50.0 1.0 CA B:ASP175 4.9 42.3 1.0

Y.Wang, F.Zhang, Y.Nie, G.Shang, H.Zhang. Structural Analysis of Shigella Flexneri Bi-Functional Enzyme Hisie in Histidine Biosynthesis. Biochem.Biophys.Res.Commun. V. 516 540 2019.
ISSN: ESSN 1090-2104
PubMed: 31235255
DOI: 10.1016/J.BBRC.2019.06.099