Magnesium in PDB 4lvm: Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (23NT). Mn-Bound Crystal Structure at pH 6.5

The structure of Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (23NT). Mn-Bound Crystal Structure at pH 6.5, PDB code: 4lvm was solved by R.Pluta, D.R.Boer, M.Coll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.40 / 3.10
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	67.340, 130.120, 87.380, 90.00, 90.00, 90.00
R / Rfree (%)	25.5 / 29.4

The structure of Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (23NT). Mn-Bound Crystal Structure at pH 6.5 also contains other interesting chemical elements:

Manganese	(Mn)	2 atoms
Chlorine	(Cl)	5 atoms
Sodium	(Na)	1 atom

The binding sites of Magnesium atom in the Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (23NT). Mn-Bound Crystal Structure at pH 6.5 (pdb code 4lvm). 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 Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (23NT). Mn-Bound Crystal Structure at pH 6.5, PDB code: 4lvm:

Magnesium binding site 1 out of 1 in the Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (23NT). Mn-Bound Crystal Structure at pH 6.5


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (23NT). Mn-Bound Crystal Structure at pH 6.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg202 b:63.3 occ:1.00 O A:MET199 2.0 0.7 1.0 C A:MET199 3.0 0.4 1.0 OXT A:MET199 3.2 0.6 1.0 CA A:MET199 4.3 0.8 1.0 CB A:MET199 4.8 0.6 1.0 N A:MET199 4.9 0.8 1.0

R.Pluta, D.R.Boer, S.Russi, C.Fernandez-Lopez, F.Lorenzo-Diaz, R.Perez-Luque, M.Espinosa, M.Coll. Structures of Dna-Mobm Relaxase Complexes Reveal A Histidine/Metal Catalysis For Dna Cleavage and Ligation To Be Published.