Magnesium in PDB 4i9g: Crystal Structure of Glycerol Phosphate Phosphatase RV1692 From Mycobacterium Tuberculosis in Complex with Magnesium

The structure of Crystal Structure of Glycerol Phosphate Phosphatase RV1692 From Mycobacterium Tuberculosis in Complex with Magnesium, PDB code: 4i9g was solved by T.Biswas, G.Larrouy-Maumus, L.P.De Carvalho, O.V.Tsodikov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 3.25
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	114.368, 71.196, 94.621, 90.00, 105.52, 90.00
R / Rfree (%)	22 / 27.2

The binding sites of Magnesium atom in the Crystal Structure of Glycerol Phosphate Phosphatase RV1692 From Mycobacterium Tuberculosis in Complex with Magnesium (pdb code 4i9g). 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 Glycerol Phosphate Phosphatase RV1692 From Mycobacterium Tuberculosis in Complex with Magnesium, PDB code: 4i9g:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Glycerol Phosphate Phosphatase RV1692 From Mycobacterium Tuberculosis in Complex with 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 Glycerol Phosphate Phosphatase RV1692 From Mycobacterium Tuberculosis in Complex with Magnesium within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg400 b:76.4 occ:1.00 OD2 A:ASP14 2.2 81.0 1.0 OD2 A:ASP209 2.2 81.6 1.0 O A:ASP16 2.2 79.9 1.0 CG A:ASP14 3.1 85.2 1.0 CG A:ASP209 3.2 79.8 1.0 OD1 A:ASP14 3.3 89.2 1.0 C A:ASP16 3.4 83.6 1.0 OD1 A:ASP209 3.4 76.8 1.0 O A:HOH501 3.9 68.3 1.0 OD2 A:ASP214 3.9 88.6 1.0 CA A:ASP16 4.2 86.3 1.0 N A:ASP16 4.4 84.4 1.0 CB A:ASP16 4.4 90.3 1.0 N A:GLY17 4.4 82.1 1.0 CB A:ASP14 4.4 83.7 1.0 CB A:ARG210 4.5 87.1 1.0 CB A:ASP209 4.5 79.1 1.0 CA A:GLY17 4.6 81.1 1.0 CD A:ARG210 4.7 92.0 1.0 OG1 A:THR18 4.7 77.6 1.0 N A:ASP209 4.8 78.6 1.0 CG A:ASP214 4.9 89.2 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Glycerol Phosphate Phosphatase RV1692 From Mycobacterium Tuberculosis in Complex with 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 Glycerol Phosphate Phosphatase RV1692 From Mycobacterium Tuberculosis in Complex with Magnesium within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg400 b:98.6 occ:1.00 OD2 B:ASP14 2.2 98.7 1.0 O B:ASP16 2.2 0.7 1.0 OD2 B:ASP209 2.2 97.3 1.0 CG B:ASP209 2.9 97.3 1.0 OD1 B:ASP209 2.9 96.0 1.0 CG B:ASP14 3.2 0.1 1.0 C B:ASP16 3.4 0.0 1.0 OD1 B:ASP14 3.5 0.0 1.0 O B:HOH501 3.5 77.3 1.0 OD2 B:ASP214 4.0 0.4 1.0 CA B:ASP16 4.2 0.2 1.0 CB B:ASP16 4.3 0.5 1.0 N B:ASP16 4.3 0.4 1.0 CB B:ASP209 4.4 98.1 1.0 N B:GLY17 4.4 0.7 1.0 CB B:ARG210 4.4 98.1 1.0 CB B:ASP14 4.5 0.1 1.0 OG1 B:THR18 4.6 1.0 1.0 CA B:GLY17 4.6 0.7 1.0 N B:ASP209 4.8 96.9 1.0 CD B:ARG210 4.9 99.4 1.0 N B:ARG210 4.9 98.9 1.0 CG2 B:VAL232 5.0 97.0 1.0

G.Larrouy-Maumus, T.Biswas, D.M.Hunt, G.Kelly, O.V.Tsodikov, L.P.De Carvalho. Discovery of A Glycerol 3-Phosphate Phosphatase Reveals Glycerophospholipid Polar Head Recycling in Mycobacterium Tuberculosis. Proc.Natl.Acad.Sci.Usa V. 110 11320 2013.
ISSN: ISSN 0027-8424
PubMed: 23801751
DOI: 10.1073/PNAS.1221597110