Magnesium in PDB 7b9p: Structure of Ribonucleotide Reductase From Rhodobacter Sphaeroides

All present enzymatic activity of Structure of Ribonucleotide Reductase From Rhodobacter Sphaeroides:
1.17.4.1;

The structure of Structure of Ribonucleotide Reductase From Rhodobacter Sphaeroides, PDB code: 7b9p was solved by P.Wilk, C.Feiler, C.Loderer, F.Kabinger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.86 / 2.65
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	140.748, 140.748, 364.277, 90, 90, 120
R / Rfree (%)	23 / 27.2

The binding sites of Magnesium atom in the Structure of Ribonucleotide Reductase From Rhodobacter Sphaeroides (pdb code 7b9p). 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 Structure of Ribonucleotide Reductase From Rhodobacter Sphaeroides, PDB code: 7b9p:

Magnesium binding site 1 out of 1 in the Structure of Ribonucleotide Reductase From Rhodobacter Sphaeroides


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Ribonucleotide Reductase From Rhodobacter Sphaeroides within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1002 b:121.2 occ:1.00 O1A A:DTP1001 2.0 123.7 0.9 O3G A:DTP1001 2.2 133.2 0.9 O1G A:DTP1001 2.3 143.1 0.9 PG A:DTP1001 2.7 129.7 0.9 O A:HOH1137 3.0 96.3 1.0 PA A:DTP1001 3.3 122.9 0.9 OG A:SER246 3.6 161.3 1.0 O5' A:DTP1001 3.7 104.9 0.9 O3B A:DTP1001 3.8 146.4 0.9 O2G A:DTP1001 3.9 120.1 0.9 CD1 A:LEU245 3.9 114.2 1.0 O3A A:DTP1001 4.1 144.5 0.9 O2B A:DTP1001 4.2 147.4 0.9 CB A:LEU245 4.2 120.8 1.0 PB A:DTP1001 4.4 147.5 0.9 N A:GLY247 4.5 156.4 1.0 O2A A:DTP1001 4.5 118.7 0.9 CG A:LEU245 4.5 116.5 1.0 C8 A:DTP1001 4.6 101.8 0.9 N A:SER246 4.7 140.2 1.0 CB A:SER246 4.8 150.6 1.0 CD2 A:LEU245 4.9 98.7 1.0 N7 A:DTP1001 4.9 102.6 0.9 C A:LEU245 5.0 122.9 1.0

T.Fietze, P.Wilk, F.Kabinger, S.Anoosheh, A.Hofer, D.Lundin, C.G.Feiler, M.S.Weiss, C.Loderer. Hug Domain Is Responsible For Active Dimer Stabilization in An Nrdjd Ribonucleotide Reductase. Biochemistry V. 61 1633 2022.
ISSN: ISSN 0006-2960
PubMed: 35856337
DOI: 10.1021/ACS.BIOCHEM.2C00173