Magnesium in PDB 6nhl: Crystal Structure of Quee From Escherichia Coli

All present enzymatic activity of Crystal Structure of Quee From Escherichia Coli:
4.3.99.3;

The structure of Crystal Structure of Quee From Escherichia Coli, PDB code: 6nhl was solved by T.A.J.Grell, B.N.Bell, C.Nguyen, D.P.Dowling, C.L.Drennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.85 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.264, 74.493, 103.714, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 22.6

The structure of Crystal Structure of Quee From Escherichia Coli also contains other interesting chemical elements:

Iron

(Fe)

9 atoms

The binding sites of Magnesium atom in the Crystal Structure of Quee From Escherichia Coli (pdb code 6nhl). 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 Quee From Escherichia Coli, PDB code: 6nhl:

Magnesium binding site 1 out of 1 in the Crystal Structure of Quee From Escherichia Coli


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 Quee From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:17.7 occ:1.00 O B:HOH445 2.0 22.6 1.0 O B:HOH547 2.0 16.9 1.0 O B:HOH457 2.1 13.4 1.0 O B:HOH552 2.1 18.9 1.0 O B:HOH561 2.1 24.9 1.0 O B:HOH426 3.9 18.6 1.0 O B:HOH501 3.9 22.0 1.0 OE1 B:GLN2 4.2 23.5 1.0 O2 B:GOL303 4.2 52.4 1.0 O1 B:GOL303 4.4 53.9 1.0 O B:HOH429 4.4 20.6 1.0 OD2 B:ASP74 4.5 20.9 1.0 NE2 B:GLN2 4.6 23.0 1.0 CD B:GLN2 4.6 29.6 1.0

T.A.J.Grell, B.N.Bell, C.Nguyen, D.P.Dowling, N.A.Bruender, V.Bandarian, C.L.Drennan. Crystal Structure of Adomet Radical Enzyme 7-Carboxy-7-Deazaguanine Synthase From Escherichia Coli Suggests How Modifications Near [4FE-4S] Cluster Engender Flavodoxin Specificity. Protein Sci. V. 28 202 2019.
ISSN: ESSN 1469-896X
PubMed: 30341796
DOI: 10.1002/PRO.3529