Chlorine 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:

Magnesium

(Mg)

1 atom

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Helicase Domain of Reverse Gyrase From Thermotoga Maritima, PDB code: 3p4x:

Chlorine 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 Chlorine with other atoms in the Cl binding site number 1 of Helicase Domain of Reverse Gyrase From Thermotoga Maritima within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1 b:87.6 occ:1.00 OG1 B:THR108 2.9 66.1 1.0 N B:GLY105 3.3 78.1 1.0 N B:THR108 3.4 59.6 1.0 NH2 B:ARG140 3.4 90.2 1.0 CA B:GLY105 3.8 78.4 1.0 CB B:THR108 3.9 49.4 1.0 CB B:THR107 3.9 53.6 1.0 N B:THR107 3.9 57.2 1.0 C B:GLY105 4.1 77.3 1.0 CA B:THR108 4.2 71.1 1.0 N B:LYS106 4.2 73.1 1.0 CA B:THR107 4.2 47.9 1.0 C B:THR107 4.2 57.4 1.0 C B:VAL104 4.5 82.6 1.0 CZ B:ARG140 4.5 95.0 1.0 O B:GLY103 4.6 81.3 1.0 NH1 B:ARG140 4.6 0.4 1.0 CA B:VAL104 4.6 87.0 1.0 O B:GLY105 4.7 67.5 1.0 CG2 B:THR107 4.8 46.2 1.0 C B:LYS106 4.8 57.5 1.0 OG1 B:THR107 4.8 62.2 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