Chlorine 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:

Manganese

(Mn)

1 atom

The binding sites of Chlorine 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 Chlorine atom.
In total 3 binding sites of Chlorine where 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:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 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 Chlorine with other atoms in the Cl 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:Cl202 b:53.6 occ:1.00 N A:ALA190 3.1 30.8 1.0 CB A:ALA190 3.2 34.9 1.0 CA A:ALA190 3.7 34.1 1.0 CB A:THR188 3.8 27.2 1.0 OG1 A:THR188 3.8 29.8 1.0 N A:VAL189 3.8 26.2 1.0 CB A:VAL189 4.0 26.1 1.0 C A:VAL189 4.0 30.0 1.0 CA A:VAL189 4.1 27.0 1.0 C A:THR188 4.4 27.3 1.0 CA A:THR188 4.7 26.2 1.0 O A:HOH425 4.7 39.5 1.0 CG2 A:THR188 4.9 27.0 1.0 CG1 A:VAL189 4.9 27.5 1.0 CG2 A:VAL189 4.9 24.2 1.0 C A:ALA190 4.9 35.8 1.0

Chlorine binding site 2 out of 3 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 Chlorine with other atoms in the Cl binding site number 2 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:Cl203 b:62.3 occ:1.00 N A:ASP50 3.1 44.3 1.0 CB A:ASP50 3.6 51.2 1.0 CA A:ARG49 3.9 38.9 1.0 CA A:ASP50 4.0 47.0 1.0 C A:ARG49 4.0 41.2 1.0 CB A:ARG49 4.1 34.7 1.0 O A:HOH383 4.2 49.8 1.0 O A:ASP50 4.4 43.7 1.0 NE2 A:GLN58 4.4 27.8 1.0 CG A:GLN58 4.6 27.7 1.0 CD A:GLN58 4.6 27.5 1.0 C A:ASP50 4.7 44.6 1.0 CB A:VAL53 4.7 39.3 1.0 CG1 A:VAL53 4.9 37.0 1.0 CB A:GLN58 4.9 28.6 1.0 O A:HOH418 5.0 6.9 0.5 CG2 A:VAL53 5.0 43.0 1.0

Chlorine binding site 3 out of 3 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 Chlorine with other atoms in the Cl binding site number 3 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:Cl204 b:71.5 occ:1.00 CB A:ASN70 3.1 53.4 1.0 N A:ASN70 3.1 46.9 1.0 ND2 A:ASN70 3.3 62.5 1.0 CG A:ASN70 3.4 59.4 1.0 CA A:ASN70 3.7 49.5 1.0 C A:SER69 4.2 44.2 1.0 OG A:SER69 4.2 42.6 1.0 OD1 A:ASN70 4.3 61.6 1.0 CA A:SER69 4.4 42.7 1.0 N A:ARG71 4.5 45.0 1.0 C A:ASN70 4.5 47.4 1.0 CB A:SER69 4.8 41.1 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.