Magnesium in PDB 6e53: Structure of Tert in Complex with A Novel Telomerase Inhibitor

All present enzymatic activity of Structure of Tert in Complex with A Novel Telomerase Inhibitor:
2.7.7.49;

The structure of Structure of Tert in Complex with A Novel Telomerase Inhibitor, PDB code: 6e53 was solved by W.Hernandez-Sanchez, W.Huang, B.Plucinsky, N.Garcia-Vazquez, A.J.Berdis, E.Skordalakes, D.J.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.99 / 2.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	80.020, 52.100, 100.480, 90.00, 98.45, 90.00
R / Rfree (%)	23 / 28.8

The binding sites of Magnesium atom in the Structure of Tert in Complex with A Novel Telomerase Inhibitor (pdb code 6e53). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Tert in Complex with A Novel Telomerase Inhibitor, PDB code: 6e53:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Tert in Complex with A Novel Telomerase Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Tert in Complex with A Novel Telomerase Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:39.4 occ:1.00 O1A A:HUV603 2.1 70.0 1.0 O2B A:HUV603 2.2 73.3 1.0 OD2 A:ASP251 2.2 45.5 1.0 O A:ILE252 2.3 50.7 1.0 O1G A:HUV603 2.5 73.0 1.0 OD1 A:ASP251 2.6 51.5 1.0 CG A:ASP251 2.7 45.3 1.0 CG A:ASP343 3.2 44.3 1.0 OD1 A:ASP343 3.4 51.4 1.0 C A:ILE252 3.4 34.5 1.0 PB A:HUV603 3.4 66.9 1.0 CB A:ASP343 3.5 40.3 1.0 OD2 A:ASP343 3.5 77.7 1.0 PA A:HUV603 3.5 91.0 1.0 PG A:HUV603 3.8 61.6 1.0 N A:ILE252 3.9 19.6 1.0 O3B A:HUV603 3.9 62.4 1.0 O3A A:HUV603 4.0 66.7 1.0 CB A:ASP251 4.1 31.8 1.0 C A:ASP251 4.2 31.5 1.0 CA A:ILE252 4.3 29.2 1.0 N A:ARG253 4.4 35.6 1.0 MG A:MG602 4.4 45.0 1.0 C5' A:HUV603 4.5 68.9 1.0 CA A:ARG253 4.5 36.2 1.0 O5' A:HUV603 4.5 87.4 1.0 N A:ASP254 4.6 41.7 1.0 CA A:ASP251 4.6 30.7 1.0 NZ A:LYS372 4.6 56.5 1.0 O2A A:HUV603 4.6 1.0 1.0 O2G A:HUV603 4.6 61.3 1.0 O1B A:HUV603 4.7 61.6 1.0 C A:ARG253 4.8 46.1 1.0 O A:ASP251 4.8 28.9 1.0 O3G A:HUV603 4.8 69.7 1.0 N A:ALA255 4.8 41.0 1.0 O A:ASP343 4.8 37.0 1.0 CB A:ILE252 4.9 32.2 1.0 CA A:ASP343 4.9 40.4 1.0 CB A:ALA255 4.9 48.4 1.0

Magnesium binding site 2 out of 2 in the Structure of Tert in Complex with A Novel Telomerase Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Tert in Complex with A Novel Telomerase Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:45.0 occ:1.00 OD2 A:ASP344 2.4 59.1 1.0 OD1 A:ASP251 2.5 51.5 1.0 O3' E:DA23 2.6 86.4 1.0 OD1 A:ASP343 2.7 51.4 1.0 OD1 A:ASP344 2.9 31.9 1.0 CG A:ASP344 3.0 34.3 1.0 OP1 E:DA23 3.5 92.3 1.0 O1A A:HUV603 3.6 70.0 1.0 CG A:ASP251 3.6 45.3 1.0 C3' E:DA23 3.7 0.6 1.0 CG A:ASP343 3.8 44.3 1.0 O2A A:HUV603 4.1 1.0 1.0 PA A:HUV603 4.3 91.0 1.0 OD2 A:ASP343 4.3 77.7 1.0 CB A:ASP251 4.4 31.8 1.0 MG A:MG601 4.4 39.4 1.0 C4' E:DA23 4.4 0.6 1.0 C5' E:DA23 4.5 0.2 1.0 CB A:ASP344 4.5 29.0 1.0 OD2 A:ASP251 4.5 45.5 1.0 O5' A:HUV603 4.6 87.4 1.0 C5' A:HUV603 4.8 68.9 1.0 NZ A:LYS372 4.8 56.5 1.0 P E:DA23 4.8 87.7 1.0 C2' E:DA23 4.9 0.9 1.0

W.Hernandez-Sanchez, W.Huang, B.Plucinsky, N.Garcia-Vazquez, N.J.Robinson, W.P.Schiemann, A.J.Berdis, E.Skordalakes, D.J.Taylor. A Non-Natural Nucleotide Uses A Specific Pocket to Selectively Inhibit Telomerase Activity. Plos Biol. V. 17 00204 2019.
ISSN: ESSN 1545-7885
PubMed: 30951520
DOI: 10.1371/JOURNAL.PBIO.3000204