Sodium in PDB 1mx0: Structure of Topoisomerase Subunit

All present enzymatic activity of Structure of Topoisomerase Subunit:
5.99.1.3;

The structure of Structure of Topoisomerase Subunit, PDB code: 1mx0 was solved by K.D.Corbett, J.M.Berger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.30
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	146.655, 219.192, 106.921, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 26.3

The structure of Structure of Topoisomerase Subunit also contains other interesting chemical elements:

Magnesium

(Mg)

6 atoms

The binding sites of Sodium atom in the Structure of Topoisomerase Subunit (pdb code 1mx0). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structure of Topoisomerase Subunit, PDB code: 1mx0:

Sodium binding site 1 out of 1 in the Structure of Topoisomerase Subunit


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Topoisomerase Subunit within 5.0Å range: probe atom residue distance (Å) B Occ D:Na901 b:78.3 occ:1.00 O D:PHE262 2.2 16.9 1.0 O D:HOH954 2.3 57.5 1.0 O D:ILE265 2.5 16.4 1.0 O D:VAL259 2.5 18.9 1.0 C D:PHE262 3.4 16.3 1.0 C D:ILE265 3.5 15.7 1.0 O D:HOH951 3.5 64.8 1.0 O D:HOH974 3.5 52.5 1.0 N D:ILE265 3.6 14.9 1.0 C D:VAL259 3.6 18.7 1.0 CA D:ILE265 3.9 14.5 1.0 CA D:GLN263 3.9 14.9 1.0 NZ D:LYS230 4.0 25.3 1.0 CB D:ILE265 4.0 13.2 1.0 CA D:VAL259 4.1 18.4 1.0 N D:GLN263 4.1 14.9 1.0 C D:GLN263 4.2 15.8 1.0 N D:SER264 4.3 15.8 1.0 O D:LEU258 4.4 17.8 1.0 CA D:PHE262 4.5 15.9 1.0 CG1 D:VAL259 4.5 17.2 1.0 N D:PHE262 4.6 17.1 1.0 N D:GLY266 4.6 16.2 1.0 CG2 D:ILE265 4.8 13.7 1.0 N D:ASN260 4.8 18.7 1.0 O D:GLN263 4.8 15.7 1.0 C D:SER264 4.8 15.6 1.0 CB D:VAL259 5.0 19.1 1.0

K.D.Corbett, J.M.Berger. Structure of the Topoisomerase VI-B Subunit: Implications For Type II Topoisomerase Mechanism and Evolution Embo J. V. 22 151 2003.
ISSN: ISSN 0261-4189
PubMed: 12505993
DOI: 10.1093/EMBOJ/CDG008