Magnesium in PDB 3rr7: Binary Structure of the Large Fragment of Taq Dna Polymerase Bound to An Abasic Site

All present enzymatic activity of Binary Structure of the Large Fragment of Taq Dna Polymerase Bound to An Abasic Site:
2.7.7.7;

The structure of Binary Structure of the Large Fragment of Taq Dna Polymerase Bound to An Abasic Site, PDB code: 3rr7 was solved by A.Marx, K.Diederichs, S.Obeid, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.40 / 1.95
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	109.460, 109.460, 90.427, 90.00, 90.00, 120.00
R / Rfree (%)	19.3 / 23.2

The binding sites of Magnesium atom in the Binary Structure of the Large Fragment of Taq Dna Polymerase Bound to An Abasic Site (pdb code 3rr7). 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 Binary Structure of the Large Fragment of Taq Dna Polymerase Bound to An Abasic Site, PDB code: 3rr7:

Magnesium binding site 1 out of 1 in the Binary Structure of the Large Fragment of Taq Dna Polymerase Bound to An Abasic Site


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Binary Structure of the Large Fragment of Taq Dna Polymerase Bound to An Abasic Site within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1 b:43.4 occ:1.00 O B:HOH117 2.1 38.2 1.0 O B:HOH115 2.1 22.0 1.0 O B:HOH116 2.1 31.8 1.0 O B:HOH318 2.1 47.2 1.0 O B:HOH61 2.1 35.3 1.0 O B:HOH74 2.1 36.8 1.0 O B:HOH158 4.0 36.1 1.0 O A:HOH157 4.2 31.3 1.0 O C:HOH256 4.3 35.8 1.0 O C:HOH57 4.3 33.5 1.0 O B:HOH15 4.3 26.6 1.0 O6 B:DG108 4.4 35.1 1.0 C5 B:DC106 4.5 22.2 1.0 N7 B:DG107 4.5 20.9 1.0 O B:HOH130 4.6 36.7 1.0 O6 B:DG107 4.6 21.1 1.0 N4 C:DC209 4.8 23.5 1.0 C6 B:DC106 4.9 23.9 1.0

S.Obeid, W.Welte, K.Diederichs, A.Marx. Amino Acid Templating Mechanisms in Selection of Nucleotides Opposite Abasic Sites By A Family A Dna Polymerase. J.Biol.Chem. V. 287 14099 2012.
ISSN: ISSN 0021-9258
PubMed: 22318723
DOI: 10.1074/JBC.M111.334904