Magnesium in PDB 3f2k: Structure of the Transposase Domain of Human Histone-Lysine N-Methyltransferase Setmar

All present enzymatic activity of Structure of the Transposase Domain of Human Histone-Lysine N-Methyltransferase Setmar:
2.1.1.43;

The structure of Structure of the Transposase Domain of Human Histone-Lysine N-Methyltransferase Setmar, PDB code: 3f2k was solved by M.F.Amaya, L.Dombrovski, S.Ni, C.Bountra, J.Weigelt, C.H.Arrowsmith, A.M.Edwards, A.Botchkarev, J.Min, A.N.Plotnikov, H.Wu, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	79.31 / 1.85
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	158.826, 46.521, 61.748, 90.00, 92.04, 90.00
R / Rfree (%)	20.5 / 25.6

The binding sites of Magnesium atom in the Structure of the Transposase Domain of Human Histone-Lysine N-Methyltransferase Setmar (pdb code 3f2k). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the Transposase Domain of Human Histone-Lysine N-Methyltransferase Setmar, PDB code: 3f2k:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of the Transposase Domain of Human Histone-Lysine N-Methyltransferase Setmar


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Transposase Domain of Human Histone-Lysine N-Methyltransferase Setmar within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg227 b:20.3 occ:1.00 OD2 A:ASP130 2.0 18.9 1.0 O A:HOH259 2.0 20.2 1.0 O A:HOH242 2.2 17.8 1.0 O A:HOH241 2.2 18.6 1.0 OD1 A:ASP38 2.2 14.2 1.0 O A:HOH469 2.2 20.2 1.0 CG A:ASP130 3.1 17.9 1.0 CG A:ASP38 3.1 19.8 1.0 OD2 A:ASP38 3.4 17.7 1.0 OD1 A:ASP130 3.4 16.8 1.0 O A:HOH323 4.0 28.2 1.0 O A:HOH238 4.1 14.1 1.0 O A:HOH423 4.1 37.4 1.0 OE1 A:GLU39 4.1 18.9 1.0 O A:HOH326 4.3 29.3 1.0 O A:HOH350 4.3 46.6 1.0 CB A:ASP130 4.4 18.3 1.0 CD2 A:LEU162 4.4 18.2 1.0 O A:GLU39 4.4 17.7 1.0 N A:GLU39 4.4 17.4 1.0 O A:HOH388 4.5 36.3 1.0 CB A:ASP38 4.5 16.4 1.0 CA A:ASP38 4.9 17.3 1.0

Magnesium binding site 2 out of 2 in the Structure of the Transposase Domain of Human Histone-Lysine N-Methyltransferase Setmar


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Transposase Domain of Human Histone-Lysine N-Methyltransferase Setmar within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg227 b:29.6 occ:1.00 OD2 B:ASP130 2.0 27.9 1.0 O B:HOH230 2.1 25.0 1.0 OD1 B:ASP38 2.1 26.9 1.0 O B:HOH259 2.2 24.6 1.0 O B:HOH331 2.2 27.7 1.0 O B:HOH260 2.3 24.7 1.0 CG B:ASP130 3.0 23.4 1.0 CG B:ASP38 3.1 25.9 1.0 OD1 B:ASP130 3.3 23.6 1.0 OD2 B:ASP38 3.4 27.1 1.0 OE1 B:GLU39 3.9 28.0 1.0 O B:HOH234 4.0 21.6 1.0 O B:HOH314 4.1 30.8 1.0 O B:HOH320 4.3 43.6 1.0 CB B:ASP130 4.3 22.0 1.0 N B:GLU39 4.4 23.3 1.0 CD2 B:LEU162 4.5 25.8 1.0 CB B:ASP38 4.5 21.6 1.0 O B:GLU39 4.6 27.1 1.0 CA B:ASP38 4.9 23.8 1.0 CB B:GLU39 5.0 24.0 1.0

L.Dombrovski, M.F.Amaya, S.Ni, C.Bountra, J.Weigelt, C.H.Arrowsmith, A.M.Edwards, A.Botchkarev, J.Min, A.N.Plotnikov, H.Wu. The Crystal Structure of Transposase Domain of Human Histone-Lysine N-Methyltransferase Setmar. To Be Published.