Magnesium in PDB 4zmi: Crystal Structure of the Helical Domain of S. Pombe TAZ1

The structure of Crystal Structure of the Helical Domain of S. Pombe TAZ1, PDB code: 4zmi was solved by W.Deng, J.Wu, F.Wang, M.Lei, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.11 / 2.30
Space group	C 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	68.010, 160.102, 50.084, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 23.3

The structure of Crystal Structure of the Helical Domain of S. Pombe TAZ1 also contains other interesting chemical elements:

Cobalt

(Co)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of the Helical Domain of S. Pombe TAZ1 (pdb code 4zmi). 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 the Helical Domain of S. Pombe TAZ1, PDB code: 4zmi:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Helical Domain of S. Pombe TAZ1


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 the Helical Domain of S. Pombe TAZ1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:35.0 occ:1.00 O A:HOH533 2.4 61.9 1.0 O A:LEU297 2.4 44.1 1.0 O A:TYR299 2.4 48.6 1.0 O A:LEU294 2.7 49.4 1.0 O A:HOH537 2.9 52.0 1.0 C A:TYR299 3.6 44.2 1.0 C A:LEU297 3.6 44.8 1.0 C A:LEU294 3.7 51.8 1.0 N A:TYR299 3.9 57.5 1.0 CZ A:PHE199 4.1 50.0 1.0 CE2 A:PHE199 4.1 54.0 1.0 CA A:TYR299 4.4 42.0 1.0 N A:LEU297 4.4 42.8 1.0 CB A:LEU294 4.4 46.3 1.0 CA A:LEU294 4.4 49.8 1.0 N A:THR300 4.5 46.3 1.0 CA A:LEU297 4.5 38.0 1.0 N A:PRO298 4.6 43.3 1.0 CA A:PRO298 4.6 53.7 1.0 C A:PRO298 4.6 63.6 1.0 N A:SER295 4.7 42.0 1.0 CA A:THR300 4.7 48.4 1.0 CA A:SER295 4.8 42.8 1.0 CB A:LEU297 4.9 43.8 1.0 C A:SER295 4.9 46.1 1.0

W.Deng, J.Wu, F.Wang, J.Kanoh, P.M.Dehe, H.Inoue, J.Chen, M.Lei. Fission Yeast Telomere-Binding Protein TAZ1 Is A Functional But Not A Structural Counterpart of Human TRF1 and TRF2. Cell Res. V. 25 881 2015.
ISSN: ISSN 1001-0602
PubMed: 26088418
DOI: 10.1038/CR.2015.76