Magnesium in PDB 1peq: Ribonucleotide Reductase Protein R1E From Salmonella Typhimurium

All present enzymatic activity of Ribonucleotide Reductase Protein R1E From Salmonella Typhimurium:
1.17.4.1;

The structure of Ribonucleotide Reductase Protein R1E From Salmonella Typhimurium, PDB code: 1peq was solved by M.Uppsten, M.Farnegardh, A.Jordan, R.Eliasson, H.Eklund, U.Uhlin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.80
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	99.144, 99.144, 289.544, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 24.6

The binding sites of Magnesium atom in the Ribonucleotide Reductase Protein R1E From Salmonella Typhimurium (pdb code 1peq). 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 Ribonucleotide Reductase Protein R1E From Salmonella Typhimurium, PDB code: 1peq:

Magnesium binding site 1 out of 1 in the Ribonucleotide Reductase Protein R1E From Salmonella Typhimurium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ribonucleotide Reductase Protein R1E From Salmonella Typhimurium within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg715 b:46.3 occ:1.00 O1B A:TTP716 1.9 32.0 1.0 O2A A:TTP716 2.1 44.9 1.0 O3G A:TTP716 2.3 41.0 1.0 PB A:TTP716 2.9 41.0 1.0 PG A:TTP716 3.1 45.2 1.0 O3A A:TTP716 3.1 42.9 1.0 PA A:TTP716 3.3 43.5 1.0 O1G A:TTP716 3.4 41.8 1.0 O3B A:TTP716 3.5 42.7 1.0 NH2 A:ARG215 4.2 50.2 1.0 O1A A:TTP716 4.3 39.6 1.0 O2B A:TTP716 4.3 42.1 1.0 C5' A:TTP716 4.4 45.6 1.0 O5' A:TTP716 4.4 44.7 1.0 O A:ASP185 4.4 40.8 1.0 CB A:ASN186 4.5 38.9 1.0 O2G A:TTP716 4.5 48.6 1.0 CA A:ASN186 4.9 39.6 1.0

M.Uppsten, M.Farnegardh, A.Jordan, R.Eliasson, H.Eklund, U.Uhlin. Structure of the Large Subunit of Class Ib Ribonucleotide Reductase From Salmonella Typhimurium and Its Complexes with Allosteric Effectors. J.Mol.Biol. V. 330 87 2003.
ISSN: ISSN 0022-2836
PubMed: 12818204
DOI: 10.1016/S0022-2836(03)00538-2