Magnesium in PDB 4f2r: Dna Polymerase I Large Fragment Complex 3

All present enzymatic activity of Dna Polymerase I Large Fragment Complex 3:
2.7.7.7;

The structure of Dna Polymerase I Large Fragment Complex 3, PDB code: 4f2r was solved by W.Wang, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.98 / 1.63
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	93.220, 108.480, 150.950, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 19.2

The binding sites of Magnesium atom in the Dna Polymerase I Large Fragment Complex 3 (pdb code 4f2r). 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 Dna Polymerase I Large Fragment Complex 3, PDB code: 4f2r:

Magnesium binding site 1 out of 1 in the Dna Polymerase I Large Fragment Complex 3


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Dna Polymerase I Large Fragment Complex 3 within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg902 b:38.8 occ:1.00 O D:HOH1642 1.9 42.1 1.0 O2B D:CTP901 2.0 30.3 1.0 O D:HOH1641 2.1 39.1 1.0 O D:HOH1643 2.1 30.2 1.0 O2A D:CTP901 2.1 46.0 1.0 O2G D:CTP901 2.5 45.9 1.0 PB D:CTP901 3.0 36.5 1.0 PA D:CTP901 3.3 41.0 1.0 H D:GLN656 3.4 17.8 0.4 PG D:CTP901 3.4 33.4 1.0 H D:GLN656 3.4 17.8 0.6 O3B D:CTP901 3.5 33.7 1.0 O3A D:CTP901 3.6 49.8 1.0 HA D:SER655 3.8 19.8 0.6 HA D:SER655 3.8 18.1 0.4 O3G D:CTP901 4.0 28.8 1.0 O1A D:CTP901 4.1 46.5 1.0 O D:HOH1062 4.1 20.2 1.0 O D:TYR654 4.2 21.4 1.0 HG3 D:GLN656 4.3 20.6 1.0 N D:GLN656 4.3 14.8 1.0 O E:HOH228 4.3 47.4 1.0 O D:HOH1278 4.3 34.2 1.0 O1B D:CTP901 4.4 28.3 1.0 OD2 D:ASP653 4.4 32.1 1.0 O5' D:CTP901 4.5 42.2 1.0 O D:HOH1203 4.5 33.2 1.0 HA D:GLN656 4.7 15.6 1.0 O1G D:CTP901 4.7 27.9 1.0 CA D:SER655 4.7 16.5 0.6 CA D:SER655 4.7 15.1 0.4 HG2 D:GLN656 4.7 20.6 1.0 OD2 D:ASP830 4.8 23.3 1.0 CG D:GLN656 5.0 17.2 1.0

W.Wang, H.W.Hellinga, L.S.Beese. Structures of A High-Fidelity Dna Polymerase To Be Published.