Magnesium in PDB 1nk5: Adenine-Adenine Mismatch at the Polymerase Active Site

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

The structure of Adenine-Adenine Mismatch at the Polymerase Active Site, PDB code: 1nk5 was solved by S.J.Johnson, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.15 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	87.574, 93.389, 105.868, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 22.1

The binding sites of Magnesium atom in the Adenine-Adenine Mismatch at the Polymerase Active Site (pdb code 1nk5). 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-Adenine Mismatch at the Polymerase Active Site, PDB code: 1nk5:

Magnesium binding site 1 out of 1 in the Adenine-Adenine 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-Adenine Mismatch at the Polymerase Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg900 b:37.1 occ:1.00 OD2 A:ASP830 2.7 28.4 1.0 OD2 A:ASP653 2.8 24.4 1.0 O A:TYR654 2.9 17.1 1.0 O A:HOH2798 3.0 32.8 1.0 C5' B:DA30 3.5 57.2 1.0 O B:HOH2774 3.8 24.4 1.0 CG A:ASP653 3.8 24.0 1.0 CG A:ASP830 3.9 24.9 1.0 CB A:ASP653 3.9 20.7 1.0 C4' B:DA30 4.0 59.6 0.0 O5' B:DA30 4.0 51.8 0.6 OP2 B:DA30 4.0 49.5 0.2 C A:TYR654 4.0 18.2 1.0 O A:HOH2839 4.1 34.7 1.0 O A:HOH2781 4.3 36.5 1.0 CA A:SER655 4.6 19.3 1.0 OD1 A:ASP830 4.6 26.8 1.0 P B:DA30 4.6 49.3 0.8 N A:TYR654 4.7 18.2 1.0 C3' B:DA30 4.8 60.9 1.0 C A:ASP653 4.8 18.8 1.0 N A:SER655 4.8 18.4 1.0 N A:GLN656 4.9 18.8 1.0 CB A:ASP830 4.9 23.9 1.0 OD1 A:ASP653 4.9 23.9 1.0

S.J.Johnson, L.S.Beese. Structures of Mismatch Replication Errors Observed in A Dna Polymerase. Cell(Cambridge,Mass.) V. 116 803 2004.
ISSN: ISSN 0092-8674
PubMed: 15035983
DOI: 10.1016/S0092-8674(04)00252-1