Magnesium in PDB 3na5: Crystal Structure of A Bacterial Phosphoglucomutase, An Enzyme Important in the Virulence of Several Human Pathogens.

All present enzymatic activity of Crystal Structure of A Bacterial Phosphoglucomutase, An Enzyme Important in the Virulence of Several Human Pathogens.:
5.4.2.2;

The structure of Crystal Structure of A Bacterial Phosphoglucomutase, An Enzyme Important in the Virulence of Several Human Pathogens., PDB code: 3na5 was solved by R.Mehra-Chaudhary, L.J.Beamer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.27 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	81.466, 105.792, 126.797, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 21.8

The binding sites of Magnesium atom in the Crystal Structure of A Bacterial Phosphoglucomutase, An Enzyme Important in the Virulence of Several Human Pathogens. (pdb code 3na5). 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 Bacterial Phosphoglucomutase, An Enzyme Important in the Virulence of Several Human Pathogens., PDB code: 3na5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of A Bacterial Phosphoglucomutase, An Enzyme Important in the Virulence of Several Human Pathogens.


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 Bacterial Phosphoglucomutase, An Enzyme Important in the Virulence of Several Human Pathogens. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg547 b:18.6 occ:1.00 OD2 A:ASP304 2.0 18.0 1.0 O A:HOH550 2.0 19.2 1.0 OD1 A:ASP308 2.0 17.6 1.0 OG A:SER146 2.0 18.3 1.0 OD2 A:ASP306 2.1 23.2 1.0 OD1 A:ASP306 2.3 29.0 1.0 CG A:ASP306 2.6 19.1 1.0 CG A:ASP304 2.9 17.2 1.0 CG A:ASP308 3.0 17.5 1.0 CB A:SER146 3.2 18.9 1.0 OD1 A:ASP304 3.4 17.6 1.0 OD2 A:ASP308 3.5 20.6 1.0 CA A:SER146 3.9 17.1 1.0 CD A:ARG309 4.0 23.2 1.0 CD2 A:HIS147 4.0 20.0 0.5 CB A:ASP304 4.1 16.5 1.0 CB A:ASP306 4.1 17.2 1.0 CG A:ARG309 4.3 18.5 1.0 O A:HOH842 4.3 39.3 1.0 CB A:ASP308 4.4 18.4 1.0 O A:HOH933 4.4 26.7 1.0 O A:HOH864 4.5 34.3 1.0 N A:ASP308 4.5 17.1 1.0 N A:ARG309 4.6 17.3 1.0 NE2 A:HIS147 4.6 20.3 0.5 CB A:ARG309 4.7 17.9 1.0 C A:SER146 4.7 17.9 1.0 N A:ASP306 4.7 16.8 1.0 N A:HIS147 4.8 18.1 1.0 CA A:ASP308 4.8 18.0 1.0 NH1 A:ARG309 4.9 30.2 1.0 CA A:ASP306 4.9 16.6 1.0 C A:ASP308 4.9 18.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of A Bacterial Phosphoglucomutase, An Enzyme Important in the Virulence of Several Human Pathogens.


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 Bacterial Phosphoglucomutase, An Enzyme Important in the Virulence of Several Human Pathogens. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg547 b:21.2 occ:1.00 O B:HOH548 2.0 23.2 1.0 OD2 B:ASP304 2.0 21.2 1.0 OG B:SER146 2.0 19.9 1.0 OD1 B:ASP308 2.1 21.5 1.0 OD1 B:ASP306 2.1 23.7 1.0 OD2 B:ASP306 2.4 25.6 1.0 CG B:ASP306 2.6 20.7 1.0 CG B:ASP304 2.9 21.0 1.0 CB B:SER146 3.1 21.2 1.0 CG B:ASP308 3.1 21.3 1.0 OD2 B:ASP308 3.4 23.6 1.0 OD1 B:ASP304 3.4 19.8 1.0 CD2 B:HIS147 3.8 23.4 0.5 CD B:ARG309 3.9 26.6 1.0 CA B:SER146 3.9 19.9 1.0 CB B:ASP304 4.1 20.3 1.0 CB B:ASP306 4.1 19.5 1.0 CG B:ARG309 4.1 21.0 1.0 NE2 B:HIS147 4.2 25.5 0.5 O B:HOH677 4.3 33.7 1.0 CB B:ASP308 4.5 20.0 1.0 ND1 B:HIS147 4.5 23.6 0.5 N B:ASP308 4.5 19.9 1.0 O B:HOH666 4.6 26.9 1.0 N B:ARG309 4.6 19.5 1.0 C B:SER146 4.6 20.3 1.0 CB B:ARG309 4.7 18.5 1.0 N B:ASP306 4.7 19.2 1.0 N B:HIS147 4.7 21.2 1.0 NH1 B:ARG309 4.8 27.8 1.0 CA B:ASP306 4.9 19.1 1.0 CA B:ASP308 4.9 20.0 1.0 CG B:HIS147 4.9 24.3 0.5 C B:ASP308 5.0 20.5 1.0

R.Mehra-Chaudhary, J.Mick, J.J.Tanner, M.T.Henzl, L.J.Beamer. Crystal Structure of A Bacterial Phosphoglucomutase, An Enzyme Involved in the Virulence of Multiple Human Pathogens. Proteins V. 79 1215 2011.
ISSN: ISSN 0887-3585
PubMed: 21246636
DOI: 10.1002/PROT.22957