Magnesium in PDB 3rsr: Crystal Structure of 5-Nitp Inhibition of Yeast Ribonucleotide Reductase

All present enzymatic activity of Crystal Structure of 5-Nitp Inhibition of Yeast Ribonucleotide Reductase:
1.17.4.1;

The structure of Crystal Structure of 5-Nitp Inhibition of Yeast Ribonucleotide Reductase, PDB code: 3rsr was solved by Q.Wan, F.Mohammed, S.Jha, E.Motea, A.Berdis, C.G.Dealwis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.97 / 2.30
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	108.353, 118.208, 63.921, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 23.3

The binding sites of Magnesium atom in the Crystal Structure of 5-Nitp Inhibition of Yeast Ribonucleotide Reductase (pdb code 3rsr). 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 Crystal Structure of 5-Nitp Inhibition of Yeast Ribonucleotide Reductase, PDB code: 3rsr:

Magnesium binding site 1 out of 1 in the Crystal Structure of 5-Nitp Inhibition of Yeast Ribonucleotide Reductase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of 5-Nitp Inhibition of Yeast Ribonucleotide Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2001 b:54.3 occ:1.00 O1G A:N5P841 2.2 51.0 1.0 O A:HOH1084 2.3 34.4 1.0 O A:HOH1013 2.4 41.4 1.0 O1A A:N5P841 2.6 35.8 1.0 O A:HOH1083 2.6 55.2 1.0 PG A:N5P841 3.0 74.6 1.0 O2G A:N5P841 3.1 35.4 1.0 O3G A:N5P841 3.8 31.6 1.0 PA A:N5P841 4.1 34.7 1.0 O3B A:N5P841 4.2 41.8 1.0 NH2 A:ARG256 4.5 30.7 1.0 O1B A:N5P841 4.5 39.5 1.0 CB A:SER227 4.6 32.0 1.0 O A:ASP226 4.6 33.2 1.0 PB A:N5P841 4.8 46.7 1.0 O3A A:N5P841 4.8 40.8 1.0 O2A A:N5P841 4.9 33.8 1.0

M.F.Ahmad, Q.Wan, S.Jha, E.Motea, A.Berdis, C.Dealwis. Evaluating the Therapeutic Potential of A Non-Natural Nucleotide That Inhibits Human Ribonucleotide Reductase. Mol.Cancer Ther. V. 11 2077 2012.
ISSN: ISSN 1535-7163
PubMed: 22933704
DOI: 10.1158/1535-7163.MCT-12-0199