Magnesium in PDB 1u49: Adenine-8OXOGUANINE Mismatch at the Polymerase Active Site

All present enzymatic activity of Adenine-8OXOGUANINE Mismatch at the Polymerase Active Site:
2.7.7.7;

The structure of Adenine-8OXOGUANINE Mismatch at the Polymerase Active Site, PDB code: 1u49 was solved by G.W.Hsu, M.Ober, T.Carell, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.57 / 2.15
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	87.382, 93.397, 106.039, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 24.7

The binding sites of Magnesium atom in the Adenine-8OXOGUANINE Mismatch at the Polymerase Active Site (pdb code 1u49). 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 Adenine-8OXOGUANINE Mismatch at the Polymerase Active Site, PDB code: 1u49:

Magnesium binding site 1 out of 1 in the Adenine-8OXOGUANINE Mismatch at the Polymerase Active Site


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Adenine-8OXOGUANINE Mismatch at the Polymerase Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg920 b:30.9 occ:1.00 OD2 A:ASP830 2.6 25.3 1.0 OD1 A:ASP653 2.7 21.2 1.0 O A:TYR654 2.8 16.7 1.0 O A:HOH2525 3.1 25.8 1.0 O A:HOH2541 3.2 35.8 1.0 CG A:ASP653 3.6 20.1 1.0 CG A:ASP830 3.7 24.1 1.0 O A:HOH2512 3.7 21.0 1.0 CB A:ASP653 3.7 18.7 1.0 C A:TYR654 3.9 17.2 1.0 O A:HOH2818 3.9 31.1 1.0 OD1 A:ASP830 4.2 24.9 1.0 N A:TYR654 4.5 17.4 1.0 CA A:SER655 4.5 18.1 1.0 C A:ASP653 4.6 17.8 1.0 O A:HOH2645 4.6 28.0 1.0 N A:SER655 4.7 17.3 1.0 OD2 A:ASP653 4.7 20.8 1.0 CA A:ASP653 4.8 18.0 1.0 CB A:ASP830 4.9 22.3 1.0 CA A:TYR654 4.9 17.1 1.0 O A:ASP830 4.9 19.1 1.0 O A:ASP653 5.0 17.3 1.0

G.W.Hsu, M.Ober, T.Carell, L.S.Beese. Error-Prone Replication of Oxidatively Damaged Dna By A High-Fidelity Dna Polymerase. Nature V. 431 217 2004.
ISSN: ISSN 0028-0836
PubMed: 15322558
DOI: 10.1038/NATURE02908