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Magnesium in PDB 2ix0: Rnase II

Enzymatic activity of Rnase II

All present enzymatic activity of Rnase II:
3.1.13.1;

Protein crystallography data

The structure of Rnase II, PDB code: 2ix0 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) 62.87 / 2.44
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 56.836, 125.719, 66.244, 90.00, 111.91, 90.00
R / Rfree (%) 18.7 / 23.6

Other elements in 2ix0:

The structure of Rnase II also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Rnase II (pdb code 2ix0). 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, PDB code: 2ix0:

Magnesium binding site 1 out of 1 in 2ix0

Go back to Magnesium Binding Sites List in 2ix0
Magnesium binding site 1 out of 1 in the Rnase II


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Rnase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1646

b:55.4
occ:1.00
O A:HOH2059 2.0 50.5 1.0
OD1 A:ASP210 2.2 55.8 1.0
O A:HOH2055 2.3 69.0 1.0
O A:HOH2060 2.3 50.3 1.0
OD1 A:ASP201 2.4 45.9 1.0
CG A:ASP210 3.2 50.6 1.0
CG A:ASP201 3.2 52.6 1.0
OD2 A:ASP201 3.5 57.1 1.0
OD2 A:ASP210 3.6 50.6 1.0
N A:ASP210 4.0 46.0 1.0
N A:ASP209 4.0 50.3 1.0
CB A:MET208 4.2 59.2 1.0
O A:ASP210 4.2 41.9 1.0
CB A:ASP210 4.4 46.2 1.0
O A:HOH2058 4.4 44.4 1.0
O A:ILE200 4.4 43.0 1.0
CB A:ASP201 4.5 45.5 1.0
CB A:ASP209 4.5 52.8 1.0
CA A:ASP210 4.6 46.0 1.0
CA A:ASP209 4.7 51.5 1.0
CA A:MET208 4.8 55.6 1.0
C A:ASP210 4.8 41.5 1.0
C A:MET208 4.8 52.8 1.0
C A:ASP209 4.9 49.3 1.0

Reference:

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. 7 443 2006.
ISSN: ISSN 0028-0836
PubMed: 16957732
DOI: 10.1038/NATURE05080
Page generated: Wed Aug 14 00:19:27 2024

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