Magnesium in PDB 6br7: Beryllium Fluorinated Receiver Domain of Bfmr From Acinetobacter Baumannii

The structure of Beryllium Fluorinated Receiver Domain of Bfmr From Acinetobacter Baumannii, PDB code: 6br7 was solved by M.E.Milton, J.Cavanagh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.04 / 1.86
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	52.163, 52.163, 197.566, 90.00, 90.00, 120.00
R / Rfree (%)	14.9 / 17.8

The structure of Beryllium Fluorinated Receiver Domain of Bfmr From Acinetobacter Baumannii also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Magnesium atom in the Beryllium Fluorinated Receiver Domain of Bfmr From Acinetobacter Baumannii (pdb code 6br7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Beryllium Fluorinated Receiver Domain of Bfmr From Acinetobacter Baumannii, PDB code: 6br7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Beryllium Fluorinated Receiver Domain of Bfmr From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Beryllium Fluorinated Receiver Domain of Bfmr From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:16.6 occ:1.00 OD1 A:ASP15 2.0 18.3 1.0 OD2 A:ASP58 2.0 12.8 1.0 F3 A:BEF301 2.1 14.7 1.0 O A:HOH414 2.1 16.2 1.0 O A:HOH453 2.1 13.5 1.0 O A:MET60 2.2 15.5 1.0 CG A:ASP15 3.0 22.6 1.0 CG A:ASP58 3.1 16.9 1.0 BE A:BEF301 3.2 19.3 1.0 HB2 A:MET60 3.3 20.3 1.0 OD2 A:ASP15 3.3 26.6 1.0 C A:MET60 3.3 17.3 1.0 OD1 A:ASP58 3.6 14.7 1.0 HD23 A:LEU61 3.6 16.7 1.0 H A:ASP15 3.6 14.6 1.0 OE2 A:GLU14 3.9 14.5 1.0 H A:MET60 4.0 16.9 1.0 CB A:MET60 4.0 16.9 1.0 CA A:MET60 4.0 14.5 1.0 O A:HOH549 4.1 30.4 1.0 HA A:LEU61 4.1 17.5 1.0 F2 A:BEF301 4.2 13.7 1.0 HB3 A:MET60 4.2 20.3 1.0 N A:MET60 4.2 14.1 1.0 F1 A:BEF301 4.3 13.2 1.0 O A:HOH575 4.3 44.4 1.0 HZ2 A:LYS107 4.3 22.9 1.0 O A:HOH548 4.3 27.4 1.0 CB A:ASP15 4.3 17.5 1.0 HB3 A:ASP58 4.3 15.8 1.0 CB A:ASP58 4.4 13.2 1.0 HZ1 A:LYS107 4.4 22.9 1.0 HE3 A:MET60 4.4 33.7 1.0 N A:LEU61 4.4 17.3 1.0 N A:ASP15 4.4 12.2 1.0 H A:ASP16 4.5 19.7 1.0 HG A:LEU61 4.5 15.1 1.0 CD2 A:LEU61 4.5 13.9 1.0 HB3 A:ASP15 4.5 21.1 1.0 CD A:GLU14 4.6 18.1 1.0 HD21 A:LEU61 4.7 16.7 1.0 NZ A:LYS107 4.7 19.1 1.0 CA A:LEU61 4.7 14.6 1.0 O A:HOH495 4.8 33.2 1.0 HB2 A:ASP58 4.8 15.8 1.0 HZ3 A:LYS107 4.8 22.9 1.0 OE1 A:GLU14 4.8 16.2 1.0 HA A:GLU14 4.8 11.0 1.0 CA A:ASP15 4.9 12.9 1.0 H A:VAL59 4.9 16.5 1.0 HA A:MET60 5.0 17.4 1.0 CG A:LEU61 5.0 12.6 1.0

Magnesium binding site 2 out of 2 in the Beryllium Fluorinated Receiver Domain of Bfmr From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Beryllium Fluorinated Receiver Domain of Bfmr From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:12.2 occ:1.00 OD2 B:ASP58 2.0 10.5 1.0 F2 B:BEF301 2.0 10.8 1.0 OD1 B:ASP15 2.1 13.3 1.0 O B:MET60 2.2 13.6 1.0 O B:HOH491 2.2 12.1 1.0 O B:HOH414 2.2 12.1 1.0 CG B:ASP58 3.1 11.0 1.0 CG B:ASP15 3.1 19.5 1.0 HB2 B:MET60 3.2 19.6 1.0 BE B:BEF301 3.2 13.4 1.0 C B:MET60 3.3 13.2 1.0 OD2 B:ASP15 3.4 23.2 1.0 OD1 B:ASP58 3.5 11.4 1.0 H B:ASP15 3.6 12.4 1.0 HD23 B:LEU61 3.7 16.3 1.0 OE2 B:GLU14 3.9 13.9 1.0 CB B:MET60 3.9 16.3 1.0 H B:MET60 4.0 14.1 1.0 CA B:MET60 4.0 13.9 1.0 HA B:LEU61 4.1 18.2 1.0 O B:HOH576 4.1 27.2 1.0 F3 B:BEF301 4.2 9.6 1.0 N B:MET60 4.2 11.7 1.0 F1 B:BEF301 4.2 10.5 1.0 HZ1 B:LYS107 4.3 16.7 1.0 O B:HOH586 4.3 33.3 1.0 HB3 B:MET60 4.3 19.6 1.0 HB3 B:ASP58 4.3 14.7 1.0 CB B:ASP58 4.3 12.2 1.0 HZ3 B:LYS107 4.3 16.7 1.0 O B:HOH594 4.3 45.4 1.0 N B:LEU61 4.4 10.6 1.0 HG B:LEU61 4.4 13.4 1.0 O B:HOH519 4.4 28.2 1.0 CB B:ASP15 4.4 13.7 1.0 N B:ASP15 4.5 10.3 1.0 H B:ASP16 4.5 13.3 1.0 CD2 B:LEU61 4.6 13.6 1.0 HB3 B:ASP15 4.6 16.4 1.0 CD B:GLU14 4.7 13.1 1.0 NZ B:LYS107 4.7 13.9 1.0 HB2 B:ASP58 4.7 14.7 1.0 CA B:LEU61 4.7 15.2 1.0 HD21 B:LEU61 4.8 16.3 1.0 OE1 B:GLU14 4.8 18.3 1.0 HA B:GLU14 4.8 10.1 1.0 H B:VAL59 4.9 12.1 1.0 HZ2 B:LYS107 4.9 16.7 1.0 HA B:MET60 4.9 16.7 1.0 CA B:ASP15 5.0 12.9 1.0 CG B:LEU61 5.0 11.2 1.0

G.L.Draughn, M.E.Milton, E.A.Feldmann, B.G.Bobay, B.M.Roth, A.L.Olson, R.J.Thompson, L.A.Actis, C.Davies, J.Cavanagh. The Structure of the Biofilm-Controlling Response Regulator Bfmr From Acinetobacter Baumannii Reveals Details of Its Dna-Binding Mechanism. J. Mol. Biol. V. 430 806 2018.
ISSN: ESSN 1089-8638
PubMed: 29438671
DOI: 10.1016/J.JMB.2018.02.002