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Magnesium in PDB 5n2q: Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to 26NT PMV158 Orit Dna

Protein crystallography data

The structure of Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to 26NT PMV158 Orit Dna, PDB code: 5n2q was solved by S.Russi, D.R.Boer, M.Coll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.73 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 43.576, 52.853, 56.035, 90.00, 95.88, 90.00
R / Rfree (%) 16.6 / 23.8

Other elements in 5n2q:

The structure of Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to 26NT PMV158 Orit Dna also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to 26NT PMV158 Orit Dna (pdb code 5n2q). 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 26NT PMV158 Orit Dna, PDB code: 5n2q:

Magnesium binding site 1 out of 1 in 5n2q

Go back to Magnesium Binding Sites List in 5n2q
Magnesium binding site 1 out of 1 in the Mobm Relaxase Domain (Mobv; MOB_PRE) Bound to 26NT PMV158 Orit Dna


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 26NT PMV158 Orit Dna within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:38.2
occ:1.00
O A:HOH326 2.1 27.6 1.0
O A:LEU95 2.3 22.1 1.0
O A:PHE92 2.4 24.6 1.0
C A:PHE92 3.5 24.3 1.0
C A:LEU95 3.5 23.5 1.0
OG1 A:THR100 4.0 20.7 1.0
CA A:GLU93 4.1 28.1 1.0
N A:LEU95 4.2 24.7 1.0
N A:GLU93 4.2 25.1 1.0
CA A:LEU95 4.3 22.4 1.0
C A:GLU93 4.3 28.7 1.0
N A:ASP96 4.5 23.1 1.0
O A:GLU93 4.5 30.2 1.0
CA A:ASP96 4.5 25.1 1.0
CA A:PHE92 4.5 23.2 1.0
CB A:LEU95 4.6 21.4 1.0
CB A:PHE92 4.6 22.6 1.0
C A:ASP96 4.6 25.2 1.0
O A:ASP96 4.7 23.2 1.0
N A:LYS94 4.9 29.1 1.0

Reference:

R.Pluta, D.R.Boer, F.Lorenzo-Diaz, S.Russi, H.Gomez, C.Fernandez-Lopez, R.Perez-Luque, M.Orozco, M.Espinosa, M.Coll. Structural Basis of A Histidine-Dna Nicking/Joining Mechanism For Gene Transfer and Promiscuous Spread of Antibiotic Resistance. Proc. Natl. Acad. Sci. V. 114 E6526 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28739894
DOI: 10.1073/PNAS.1702971114
Page generated: Sun Sep 29 23:04:16 2024

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