Magnesium in PDB 2v0j: Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu)

The structure of Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu), PDB code: 2v0j was solved by I.Mochalkin, S.Lightle, J.F.Ohren, N.Y.Chirgadze, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.0
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	108.720, 108.720, 326.754, 90.00, 90.00, 120.00
R / Rfree (%)	19.7 / 22.3

The binding sites of Magnesium atom in the Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu) (pdb code 2v0j). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu), PDB code: 2v0j:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1454 b:18.9 occ:0.33 OD2 A:ASP406 2.1 16.5 1.0 O A:HOH2310 2.2 16.5 1.0 CG A:ASP406 3.1 16.0 1.0 OD1 A:ASP406 3.5 15.9 1.0 NE2 A:GLN408 4.0 19.5 1.0 O A:ASP406 4.0 18.2 1.0 MG A:MG1455 4.1 15.1 0.3 O A:HOH2320 4.1 31.6 1.0 CB A:ASP406 4.2 16.3 1.0 O A:HOH2288 4.8 17.4 1.0 C A:ASP406 4.9 16.8 1.0

Magnesium binding site 2 out of 2 in the Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-Acetylglucosamine-1- Phosphate Uridyltransferase (Glmu) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1455 b:15.1 occ:0.33 O A:HOH2309 2.1 16.0 1.0 OD1 A:ASP406 2.1 15.9 1.0 CG A:ASP406 3.2 16.0 1.0 OD2 A:ASP406 3.5 16.5 1.0 MG A:MG1454 4.1 18.9 0.3 O A:HOH2288 4.3 17.4 1.0 O A:HOH2272 4.4 21.4 1.0 O A:GLY381 4.4 15.6 1.0 CB A:ASP406 4.4 16.3 1.0 CA A:ASP406 4.9 16.1 1.0

I.Mochalkin, S.Lightle, Y.Zhu, J.F.Ohren, C.Spessard, N.Y.Chirgadze, C.Banotai, M.Melnick, L.Mcdowell. Characterization of Substrate Binding and Catalysis in the Potential Antibacterial Target N- Acetylglucosamine-1-Phosphate Uridyltransferase (Glmu). Protein Sci. V. 16 2657 2007.
ISSN: ISSN 0961-8368
PubMed: 18029420
DOI: 10.1110/PS.073135107