Magnesium in PDB 3h8s: Structure of D19N T4 Rnase H in the Presence of Divalent Magnesium

All present enzymatic activity of Structure of D19N T4 Rnase H in the Presence of Divalent Magnesium:
3.1.26.4;

The structure of Structure of D19N T4 Rnase H in the Presence of Divalent Magnesium, PDB code: 3h8s was solved by S.J.Tomanicek, T.C.Mueser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.75 / 2.51
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.312, 75.298, 88.090, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 23.4

The binding sites of Magnesium atom in the Structure of D19N T4 Rnase H in the Presence of Divalent Magnesium (pdb code 3h8s). 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 D19N T4 Rnase H in the Presence of Divalent Magnesium, PDB code: 3h8s:

Magnesium binding site 1 out of 1 in the Structure of D19N T4 Rnase H in the Presence of Divalent Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of D19N T4 Rnase H in the Presence of Divalent Magnesium within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg350 b:24.5 occ:1.00 O A:HOH353 2.0 27.7 1.0 O A:HOH351 2.1 26.6 1.0 O A:HOH348 2.2 29.2 1.0 O A:HOH352 2.2 26.0 1.0 O A:HOH349 2.2 32.7 1.0 O A:HOH354 2.5 31.1 1.0 OD2 A:ASP157 3.8 39.5 1.0 O A:LEU257 4.0 26.2 1.0 OH A:TYR86 4.1 25.1 1.0 OD2 A:ASP132 4.1 31.1 1.0 OE1 A:GLU130 4.2 28.8 1.0 O A:HOH347 4.3 32.3 1.0 OD2 A:ASP200 4.3 27.6 1.0 CE1 A:PHE260 4.5 24.1 1.0 CZ A:ARG79 4.6 28.1 1.0 NH2 A:ARG79 4.6 21.4 1.0 NH1 A:ARG79 4.7 29.6 1.0 O A:HOH337 4.7 24.6 1.0 O A:ILE258 4.8 21.7 1.0 CB A:ASP132 4.8 27.2 1.0 CG A:ASP157 4.9 38.9 1.0 O A:HOH355 4.9 40.0 1.0 CG A:ASP132 5.0 32.4 1.0 NE A:ARG79 5.0 27.0 1.0

S.J.Tomanicek, J.M.Devos, T.C.Mueser. Additional Order Appears in the Absence of Metals in A Fen-1 Protein: Structural Analysis of Magnesium Binding to Bacteriophage T4 Rnaseh To Be Published.