Magnesium in PDB 4p31: Crystal Structure of A Selenomethionine Derivative of E. Coli Lptb in Complex with Adp-Magensium

The structure of Crystal Structure of A Selenomethionine Derivative of E. Coli Lptb in Complex with Adp-Magensium, PDB code: 4p31 was solved by D.J.Sherman, M.B.Lazarus, L.Murphy, C.Liu, S.Walker, N.Ruiz, D.Kahne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.00 / 2.05
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	192.600, 35.880, 64.340, 90.00, 95.83, 90.00
R / Rfree (%)	18.5 / 23.8

The binding sites of Magnesium atom in the Crystal Structure of A Selenomethionine Derivative of E. Coli Lptb in Complex with Adp-Magensium (pdb code 4p31). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of A Selenomethionine Derivative of E. Coli Lptb in Complex with Adp-Magensium, PDB code: 4p31:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of A Selenomethionine Derivative of E. Coli Lptb in Complex with Adp-Magensium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of A Selenomethionine Derivative of E. Coli Lptb in Complex with Adp-Magensium within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:25.0 occ:1.00 O3B A:ADP401 2.1 21.6 1.0 O A:HOH556 2.1 20.4 1.0 O A:HOH555 2.1 20.9 1.0 O A:HOH557 2.1 25.6 1.0 OG1 A:THR43 2.1 20.0 1.0 OE1 A:GLN85 2.2 28.7 1.0 PB A:ADP401 3.1 24.1 1.0 CB A:THR43 3.3 23.2 1.0 CD A:GLN85 3.3 33.5 1.0 O2B A:ADP401 3.3 23.9 1.0 NE2 A:GLN85 3.7 36.0 1.0 OE2 A:GLU163 3.8 47.6 1.0 O2A A:ADP401 3.9 24.8 1.0 N A:THR43 4.0 19.2 1.0 OD1 A:ASP162 4.1 23.8 1.0 O1B A:ADP401 4.1 25.0 1.0 OD2 A:ASP162 4.2 23.5 1.0 CA A:THR43 4.2 22.4 1.0 O3A A:ADP401 4.3 24.6 1.0 CG2 A:THR43 4.4 27.4 1.0 CG A:ASP162 4.5 23.4 1.0 PA A:ADP401 4.6 26.0 1.0 CD A:GLU163 4.6 49.3 1.0 CG A:GLN85 4.6 32.8 1.0 CB A:GLN85 4.9 24.2 1.0 O A:HOH520 4.9 29.9 1.0 CE A:LYS42 4.9 21.1 1.0 CB A:LYS42 5.0 20.6 1.0 O A:HOH512 5.0 49.3 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of A Selenomethionine Derivative of E. Coli Lptb in Complex with Adp-Magensium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of A Selenomethionine Derivative of E. Coli Lptb in Complex with Adp-Magensium within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:23.2 occ:1.00 O B:HOH547 2.1 22.5 1.0 O B:HOH546 2.1 24.1 1.0 OG1 B:THR43 2.1 17.7 1.0 O B:HOH548 2.1 19.4 1.0 OE1 B:GLN85 2.2 26.9 1.0 O1B B:ADP401 2.2 22.4 1.0 CB B:THR43 3.1 14.7 1.0 CD B:GLN85 3.2 35.3 1.0 PB B:ADP401 3.3 26.3 1.0 O3B B:ADP401 3.4 30.0 1.0 NE2 B:GLN85 3.7 37.9 1.0 O1A B:ADP401 3.9 30.0 1.0 OE2 B:GLU163 3.9 47.4 1.0 N B:THR43 4.0 22.8 1.0 OD1 B:ASP162 4.0 21.2 1.0 OD2 B:ASP162 4.1 21.2 1.0 CA B:THR43 4.1 16.6 1.0 CG2 B:THR43 4.2 15.9 1.0 O B:HOH535 4.3 38.1 1.0 O2B B:ADP401 4.4 17.8 1.0 O3A B:ADP401 4.4 25.9 1.0 CG B:ASP162 4.5 17.3 1.0 CG B:GLN85 4.5 26.9 1.0 PA B:ADP401 4.6 26.3 1.0 O B:HOH518 4.7 30.6 1.0 CG B:GLU163 4.7 46.8 1.0 CD B:GLU163 4.8 50.6 1.0 CB B:GLN85 4.9 20.9 1.0

D.J.Sherman, M.B.Lazarus, L.Murphy, C.Liu, S.Walker, N.Ruiz, D.Kahne. Decoupling Catalytic Activity From Biological Function of the Atpase That Powers Lipopolysaccharide Transport. Proc.Natl.Acad.Sci.Usa V. 111 4982 2014.
ISSN: ESSN 1091-6490
PubMed: 24639492
DOI: 10.1073/PNAS.1323516111