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Manganese in PDB 4lvk: Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (22NT+3'Phosphate). Mn-Bound Crystal Structure at pH 4.6

Protein crystallography data

The structure of Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (22NT+3'Phosphate). Mn-Bound Crystal Structure at pH 4.6, PDB code: 4lvk 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) 36.93 / 2.37
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 112.743, 112.743, 91.660, 90.00, 90.00, 120.00
R / Rfree (%) 20.1 / 25

Other elements in 4lvk:

The structure of Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (22NT+3'Phosphate). Mn-Bound Crystal Structure at pH 4.6 also contains other interesting chemical elements:

Sodium (Na) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (22NT+3'Phosphate). Mn-Bound Crystal Structure at pH 4.6 (pdb code 4lvk). 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'Phosphate). Mn-Bound Crystal Structure at pH 4.6, PDB code: 4lvk:

Manganese binding site 1 out of 1 in 4lvk

Go back to Manganese Binding Sites List in 4lvk
Manganese binding site 1 out of 1 in the Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to Plasmid PMV158 Orit Dna (22NT+3'Phosphate). Mn-Bound Crystal Structure at pH 4.6


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'Phosphate). Mn-Bound Crystal Structure at pH 4.6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:40.1
occ:1.00
OE2 A:GLU129 1.9 48.8 1.0
NE2 A:HIS133 2.0 46.2 1.0
ND1 A:HIS126 2.0 46.6 1.0
NE2 A:HIS135 2.1 38.6 1.0
OP1 C:DT27 2.2 49.4 1.0
O3' C:DG26 2.6 52.2 1.0
CE1 A:HIS133 2.9 44.3 1.0
CE1 A:HIS126 2.9 46.0 1.0
P C:DT27 3.0 49.9 1.0
CE1 A:HIS135 3.0 36.8 1.0
CD2 A:HIS135 3.1 35.8 1.0
CD2 A:HIS133 3.1 38.8 1.0
CG A:HIS126 3.1 43.5 1.0
CD A:GLU129 3.2 47.0 1.0
CB A:HIS126 3.5 40.9 1.0
OP2 C:DT27 3.9 53.8 1.0
C3' C:DG26 3.9 49.6 1.0
ND1 A:HIS133 4.1 41.7 1.0
OE1 A:GLU129 4.1 47.7 1.0
NE2 A:HIS126 4.1 45.5 1.0
NH2 A:ARG25 4.1 44.0 1.0
CG A:GLU129 4.1 45.8 1.0
O5' C:DT27 4.1 48.1 1.0
ND1 A:HIS135 4.2 35.4 1.0
CG A:HIS133 4.2 41.2 1.0
CD2 A:HIS126 4.2 45.1 1.0
C2' C:DG26 4.2 47.0 1.0
CG A:HIS135 4.2 35.8 1.0
C4' C:DG26 4.4 50.7 1.0
NH1 A:ARG25 5.0 47.7 1.0

Reference:

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.
Page generated: Tue Dec 15 04:24:09 2020

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