Calcium in PDB 3uc1: Mycobacterium Tuberculosis Gyrase Type Iia Topoisomerase C-Terminal Domain

All present enzymatic activity of Mycobacterium Tuberculosis Gyrase Type Iia Topoisomerase C-Terminal Domain:
5.99.1.3;

The structure of Mycobacterium Tuberculosis Gyrase Type Iia Topoisomerase C-Terminal Domain, PDB code: 3uc1 was solved by E.M.Tretter, J.M.Berger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.72 / 1.65
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	38.871, 82.842, 83.433, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 22.2

The binding sites of Calcium atom in the Mycobacterium Tuberculosis Gyrase Type Iia Topoisomerase C-Terminal Domain (pdb code 3uc1). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Mycobacterium Tuberculosis Gyrase Type Iia Topoisomerase C-Terminal Domain, PDB code: 3uc1:

Calcium binding site 1 out of 1 in the Mycobacterium Tuberculosis Gyrase Type Iia Topoisomerase C-Terminal Domain


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Mycobacterium Tuberculosis Gyrase Type Iia Topoisomerase C-Terminal Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca901 b:17.6 occ:1.00 O A:VAL783 2.4 17.6 1.0 O A:ACT902 2.5 18.7 1.0 O A:HOH1023 2.5 19.1 1.0 OXT A:ACT902 2.6 21.8 1.0 C A:ACT902 3.0 23.5 1.0 C A:VAL783 3.5 11.7 1.0 N A:VAL783 4.0 10.9 1.0 CA A:VAL783 4.3 13.4 1.0 OXT A:ACT903 4.5 31.6 1.0 CH3 A:ACT902 4.5 27.1 1.0 N A:ILE784 4.5 14.6 1.0 CA A:ILE784 4.6 17.5 1.0 O A:ACT903 4.6 29.2 1.0 O A:HOH1186 4.6 30.3 1.0 N A:LEU549 4.8 27.0 1.0 CB A:VAL783 4.8 12.1 1.0 O A:LEU549 4.9 24.6 1.0 CG1 A:ILE784 5.0 13.9 1.0

E.M.Tretter, J.M.Berger. Mechanisms For Defining Supercoiling Set Point of Dna Gyrase Orthologs: II. the Shape of the Gyra Subunit C-Terminal Domain (Ctd) Is Not A Sole Determinant For Controlling Supercoiling Efficiency. J.Biol.Chem. V. 287 18645 2012.
ISSN: ISSN 0021-9258
PubMed: 22457352
DOI: 10.1074/JBC.M112.345736