Magnesium in PDB 2hhq: O6-Methyl-Guanine:T Pair in the Polymerase-10 Basepair Position

All present enzymatic activity of O6-Methyl-Guanine:T Pair in the Polymerase-10 Basepair Position:
2.7.7.7;

The structure of O6-Methyl-Guanine:T Pair in the Polymerase-10 Basepair Position, PDB code: 2hhq was solved by J.J.Warren, L.J.Forsberg, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.792, 93.274, 106.018, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 24.4

The binding sites of Magnesium atom in the O6-Methyl-Guanine:T Pair in the Polymerase-10 Basepair Position (pdb code 2hhq). 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 O6-Methyl-Guanine:T Pair in the Polymerase-10 Basepair Position, PDB code: 2hhq:

Magnesium binding site 1 out of 1 in the O6-Methyl-Guanine:T Pair in the Polymerase-10 Basepair Position


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of O6-Methyl-Guanine:T Pair in the Polymerase-10 Basepair Position within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg920 b:35.7 occ:1.00 OD2 A:ASP653 2.6 21.5 1.0 O A:TYR654 2.8 13.9 1.0 OD2 A:ASP830 3.0 19.5 1.0 O A:HOH2814 3.1 20.9 1.0 O A:HOH3510 3.4 31.6 1.0 CG A:ASP653 3.5 21.1 1.0 CB A:ASP653 3.7 15.2 1.0 O A:HOH3085 3.8 14.8 1.0 CG A:ASP830 3.9 18.9 1.0 C A:TYR654 4.0 14.2 1.0 O A:HOH2518 4.0 28.2 1.0 OD1 A:ASP830 4.2 17.4 1.0 O B:HOH3511 4.4 35.3 1.0 O A:HOH3098 4.4 30.6 1.0 N A:TYR654 4.5 12.5 1.0 C A:ASP653 4.6 12.4 1.0 CA A:SER655 4.7 15.0 1.0 OD1 A:ASP653 4.7 21.3 1.0 N A:SER655 4.8 13.8 1.0 CA A:ASP653 4.8 13.9 1.0 CA A:TYR654 4.9 12.5 1.0 N A:GLN656 5.0 12.2 1.0

J.J.Warren, L.J.Forsberg, L.S.Beese. The Structural Basis For the Mutagenicity of O6-Methyl-Guanine Lesions. Proc.Natl.Acad.Sci.Usa V. 103 19701 2006.
ISSN: ISSN 0027-8424
PubMed: 17179038
DOI: 10.1073/PNAS.0609580103