Magnesium in PDB 2ix1: Rnase II D209N Mutant

All present enzymatic activity of Rnase II D209N Mutant:
3.1.13.1;

The structure of Rnase II D209N Mutant, PDB code: 2ix1 was solved by C.Frazao, C.E.Mcvey, M.Amblar, A.Barbas, C.Vonrhein, C.M.Arraiano, M.A.Carrondo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.30 / 2.74
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	86.316, 86.316, 279.245, 90.00, 90.00, 120.00
R / Rfree (%)	18.5 / 22.5

The binding sites of Magnesium atom in the Rnase II D209N Mutant (pdb code 2ix1). 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 Rnase II D209N Mutant, PDB code: 2ix1:

Magnesium binding site 1 out of 1 in the Rnase II D209N Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Rnase II D209N Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1644 b:51.6 occ:1.00 O A:HOH2011 2.2 53.9 1.0 O A:HOH2013 2.2 44.0 1.0 OD1 A:ASP201 2.4 45.4 1.0 OD2 A:ASP210 2.4 35.9 1.0 OP1 B:A13 2.5 38.3 1.0 O3' B:A12 2.6 35.2 1.0 P B:A13 3.0 39.3 1.0 CG A:ASP201 3.2 44.9 1.0 CG A:ASP210 3.3 34.5 1.0 OD2 A:ASP201 3.3 49.0 1.0 OD1 A:ASP210 3.6 38.8 1.0 O5' B:A13 3.6 46.9 1.0 C3' B:A12 3.8 37.5 1.0 O2' B:A12 3.9 49.6 1.0 C4' B:A12 4.1 40.0 1.0 N A:ASN209 4.1 31.3 1.0 N A:ASP210 4.1 30.9 1.0 O A:ILE200 4.2 38.0 1.0 O A:HOH2015 4.2 48.6 1.0 OP2 B:A13 4.3 49.7 1.0 C2' B:A12 4.3 36.7 1.0 O A:ASP210 4.4 39.3 1.0 O B:HOH2001 4.4 43.8 1.0 C5' B:A12 4.5 34.8 1.0 CB A:ASP210 4.5 33.5 1.0 CA A:MET208 4.6 32.5 1.0 CB A:ASP201 4.7 34.9 1.0 CA A:ASP210 4.7 32.4 1.0 C5' B:A13 4.8 51.0 1.0 C A:MET208 4.8 32.4 1.0 CA A:ASN209 4.9 31.3 1.0 CB A:ASN209 5.0 31.8 1.0 O B:HOH2002 5.0 49.4 1.0

C.Frazao, C.E.Mcvey, M.Amblar, A.Barbas, C.Vonrhein, C.M.Arraiano, M.A.Carrondo. Unravelling the Dynamics of Rna Degradation By Ribonuclease II and Its Rna-Bound Complex Nature V. 443 110 2006.
ISSN: ISSN 0028-0836
PubMed: 16957732
DOI: 10.1038/NATURE05080