Manganese in PDB 4lvl: Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (22NT+3'Thiophosphate). Mn-Bound Crystal Structure at pH 6.8

The structure of Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (22NT+3'Thiophosphate). Mn-Bound Crystal Structure at pH 6.8, PDB code: 4lvl 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)	36.80 / 2.20
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	112.420, 112.420, 90.650, 90.00, 90.00, 120.00
R / Rfree (%)	18.7 / 23.7

The structure of Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (22NT+3'Thiophosphate). Mn-Bound Crystal Structure at pH 6.8 also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Manganese atom in the Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (22NT+3'Thiophosphate). Mn-Bound Crystal Structure at pH 6.8 (pdb code 4lvl). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (22NT+3'Thiophosphate). Mn-Bound Crystal Structure at pH 6.8, PDB code: 4lvl:

Manganese binding site 1 out of 1 in the Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (22NT+3'Thiophosphate). Mn-Bound Crystal Structure at pH 6.8


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (22NT+3'Thiophosphate). Mn-Bound Crystal Structure at pH 6.8 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:17.9 occ:1.00 NE2 A:HIS133 2.2 22.0 1.0 O3' C:DG26 2.2 29.1 1.0 OE2 A:GLU129 2.3 24.3 1.0 ND1 A:HIS126 2.3 21.1 1.0 O3P C:TS6101 2.3 34.8 1.0 NE2 A:HIS135 2.4 18.0 1.0 P C:TS6101 2.8 32.5 1.0 CE1 A:HIS133 3.1 21.8 1.0 CE1 A:HIS126 3.2 21.1 1.0 CD2 A:HIS133 3.2 20.4 1.0 CE1 A:HIS135 3.3 17.8 1.0 CG A:HIS126 3.3 20.6 1.0 CD2 A:HIS135 3.4 16.8 1.0 CD A:GLU129 3.4 25.3 1.0 C3' C:DG26 3.5 26.8 1.0 CB A:HIS126 3.7 19.2 1.0 NH2 A:ARG25 3.8 27.0 1.0 O4P C:TS6101 3.9 34.7 1.0 C2' C:DG26 4.0 25.7 1.0 OE1 A:GLU129 4.0 26.4 1.0 C4' C:DG26 4.1 27.1 1.0 S2P C:TS6101 4.3 36.4 1.0 ND1 A:HIS133 4.3 21.8 1.0 NE2 A:HIS126 4.3 20.4 1.0 O C:HOH226 4.3 41.7 1.0 CG A:HIS133 4.3 20.4 1.0 CD2 A:HIS126 4.4 19.9 1.0 ND1 A:HIS135 4.4 17.0 1.0 CG A:HIS135 4.5 16.7 1.0 CG A:GLU129 4.6 25.3 1.0 NH1 A:ARG25 4.6 26.4 1.0 CZ A:ARG25 4.7 27.3 1.0 C1' C:DG26 5.0 25.1 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.