Magnesium in PDB 3p4x: Helicase Domain of Reverse Gyrase From Thermotoga Maritima

The structure of Helicase Domain of Reverse Gyrase From Thermotoga Maritima, PDB code: 3p4x was solved by M.G.Rudolph, D.Klostermeier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.03 / 2.41
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.259, 111.231, 129.726, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 25.6

The structure of Helicase Domain of Reverse Gyrase From Thermotoga Maritima also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Helicase Domain of Reverse Gyrase From Thermotoga Maritima (pdb code 3p4x). 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 Helicase Domain of Reverse Gyrase From Thermotoga Maritima, PDB code: 3p4x:

Magnesium binding site 1 out of 1 in the Helicase Domain of Reverse Gyrase From Thermotoga Maritima


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Helicase Domain of Reverse Gyrase From Thermotoga Maritima within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg799 b:91.0 occ:1.00 O A:HOH35 2.5 83.2 1.0 OG1 A:THR107 2.5 68.6 1.0 O A:HOH33 2.6 61.8 1.0 O1B A:ADP800 2.6 0.3 1.0 O A:HOH34 2.6 68.5 1.0 O A:HOH32 2.7 71.8 1.0 O3B A:ADP800 3.3 0.1 1.0 PB A:ADP800 3.5 0.1 1.0 CB A:THR107 3.6 58.0 1.0 OD1 A:ASP203 3.9 86.6 1.0 O2A A:ADP800 4.1 0.3 1.0 N A:THR107 4.2 58.8 1.0 OD2 A:ASP203 4.3 98.6 1.0 CA A:THR107 4.5 50.1 1.0 O3A A:ADP800 4.5 98.2 1.0 CG A:ASP203 4.5 91.5 1.0 O2B A:ADP800 4.7 96.6 1.0 CG2 A:THR107 4.7 49.7 1.0 PA A:ADP800 4.7 0.1 1.0

Y.Del Toro Duany, D.Klostermeier, M.G.Rudolph. The Conformational Flexibility of the Helicase-Like Domain From Thermotoga Maritima Reverse Gyrase Is Restricted By the Topoisomerase Domain. Biochemistry V. 50 5816 2011.
ISSN: ISSN 0006-2960
PubMed: 21627332
DOI: 10.1021/BI200236A