Magnesium in PDB 6ge9: Structure of Mycobacterium Tuberculosis Glmu Bound to Glc-1P and Ac- Coa

All present enzymatic activity of Structure of Mycobacterium Tuberculosis Glmu Bound to Glc-1P and Ac- Coa:
2.3.1.157; 2.7.7.23;

The structure of Structure of Mycobacterium Tuberculosis Glmu Bound to Glc-1P and Ac- Coa, PDB code: 6ge9 was solved by P.D.Craggs, S.Mouilleron, M.Rejzek, C.De Chiara, R.J.Young, R.A.Field, A.Argyrou, L.P.S.De Carvalho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.13 / 2.26
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	109.753, 109.753, 364.894, 90.00, 90.00, 120.00
R / Rfree (%)	24.3 / 27.7

The binding sites of Magnesium atom in the Structure of Mycobacterium Tuberculosis Glmu Bound to Glc-1P and Ac- Coa (pdb code 6ge9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of Mycobacterium Tuberculosis Glmu Bound to Glc-1P and Ac- Coa, PDB code: 6ge9:

Magnesium binding site 1 out of 1 in the Structure of Mycobacterium Tuberculosis Glmu Bound to Glc-1P and Ac- Coa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Mycobacterium Tuberculosis Glmu Bound to Glc-1P and Ac- Coa within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:72.5 occ:0.33 OG A:SER392 2.3 61.7 1.0 OD1 A:ASP417 2.8 58.6 1.0 CB A:SER392 3.7 43.0 1.0 O A:SER392 3.7 42.3 1.0 CG A:ASP417 3.8 54.4 1.0 CB A:ASP417 4.6 43.6 1.0 CA A:SER392 4.6 35.1 1.0 C A:SER392 4.6 39.6 1.0 OD2 A:ASP417 4.7 60.4 1.0

P.D.Craggs, S.Mouilleron, M.Rejzek, C.De Chiara, R.J.Young, R.A.Field, A.Argyrou, L.P.S.De Carvalho. The Mechanism of Acetyl Transfer Catalyzed By Mycobacterium Tuberculosis Glmu. Biochemistry V. 57 3387 2018.
ISSN: ISSN 1520-4995
PubMed: 29684272
DOI: 10.1021/ACS.BIOCHEM.8B00121