Magnesium in PDB 4p32: Crystal Structure of E. Coli Lptb in Complex with Adp-Magnesium

The structure of Crystal Structure of E. Coli Lptb in Complex with Adp-Magnesium, PDB code: 4p32 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)	31.80 / 1.55
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	191.900, 36.020, 64.510, 90.00, 96.16, 90.00
R / Rfree (%)	19.8 / 21.8

The binding sites of Magnesium atom in the Crystal Structure of E. Coli Lptb in Complex with Adp-Magnesium (pdb code 4p32). 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 E. Coli Lptb in Complex with Adp-Magnesium, PDB code: 4p32:
Jump to Magnesium binding site number: 1; 2;

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


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 E. Coli Lptb in Complex with Adp-Magnesium within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:20.5 occ:1.00 O1B A:ADP401 2.1 20.2 1.0 O A:HOH556 2.1 22.8 1.0 OG1 A:THR43 2.1 23.7 1.0 O A:HOH558 2.1 19.6 1.0 OE1 A:GLN85 2.1 21.7 1.0 O A:HOH557 2.2 20.1 1.0 CD A:GLN85 3.1 26.1 1.0 CB A:THR43 3.2 20.8 1.0 PB A:ADP401 3.3 20.3 1.0 O2B A:ADP401 3.5 21.1 1.0 NE2 A:GLN85 3.6 30.8 1.0 OE2 A:GLU163 3.7 33.6 1.0 O1A A:ADP401 3.9 22.8 1.0 N A:THR43 3.9 20.1 1.0 OD1 A:ASP162 4.0 22.5 1.0 CA A:THR43 4.1 20.4 1.0 O A:HOH586 4.1 40.1 1.0 OD2 A:ASP162 4.2 19.8 1.0 CG2 A:THR43 4.3 18.2 1.0 O3B A:ADP401 4.3 21.5 1.0 O3A A:ADP401 4.3 21.5 1.0 CG A:ASP162 4.5 22.4 1.0 CG A:GLN85 4.5 26.8 1.0 PA A:ADP401 4.6 21.6 1.0 CD A:GLU163 4.6 35.4 1.0 CB A:GLN85 4.7 23.4 1.0 O A:HOH526 4.8 28.2 1.0 CB A:LYS42 4.9 21.6 1.0

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


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 E. Coli Lptb in Complex with Adp-Magnesium within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:16.2 occ:1.00 O2B B:ADP401 2.0 16.6 1.0 O B:HOH555 2.0 16.4 1.0 O B:HOH553 2.1 19.5 1.0 OG1 B:THR43 2.1 15.5 1.0 O B:HOH554 2.1 19.2 1.0 OE1 B:GLN85 2.1 19.4 1.0 CB B:THR43 3.1 14.9 1.0 CD B:GLN85 3.2 25.0 1.0 PB B:ADP401 3.3 17.9 1.0 O3B B:ADP401 3.5 20.6 1.0 NE2 B:GLN85 3.6 27.8 1.0 OE2 B:GLU163 3.8 28.6 1.0 N B:THR43 3.9 13.8 1.0 O1A B:ADP401 4.0 18.2 1.0 OD1 B:ASP162 4.0 19.4 1.0 CA B:THR43 4.0 13.1 1.0 OD2 B:ASP162 4.1 17.3 1.0 CG2 B:THR43 4.2 14.6 1.0 O3A B:ADP401 4.3 18.9 1.0 O B:HOH546 4.3 28.2 1.0 O1B B:ADP401 4.3 18.1 1.0 CG B:ASP162 4.5 16.9 1.0 CG B:GLN85 4.5 25.6 1.0 PA B:ADP401 4.6 17.8 1.0 CD B:GLU163 4.7 29.7 1.0 CB B:GLN85 4.8 24.4 1.0 O B:HOH529 4.8 25.6 1.0 CB B:LYS42 4.9 15.0 1.0 C B:LYS42 5.0 13.6 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