Magnesium in PDB 3dk5: Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis

All present enzymatic activity of Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis:
2.3.1.157; 2.7.7.23;

The structure of Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis, PDB code: 3dk5 was solved by S.K.Verma, B.Prakash, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.30 / 2.23
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	79.600, 79.600, 278.000, 90.00, 90.00, 120.00
R / Rfree (%)	22.5 / 27.1

The binding sites of Magnesium atom in the Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis (pdb code 3dk5). 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 Apo-Glmu From Mycobacterium Tuberculosis, PDB code: 3dk5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis


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 Apo-Glmu From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg496 b:18.0 occ:0.33 OD2 A:ASP417 2.6 27.5 1.0 O A:HOH530 3.6 26.5 1.0 CG A:ASP417 3.7 32.6 1.0 OD1 A:ASP417 4.0 36.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis


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 Apo-Glmu From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg497 b:26.3 occ:0.33 OD1 A:ASP417 3.1 36.5 1.0 OG A:SER392 3.8 37.2 1.0 CG A:ASP417 4.2 32.6 1.0 OD2 A:ASP417 4.7 27.5 1.0 O A:SER392 4.9 25.9 1.0

A.Parikh, S.K.Verma, S.Khan, B.Prakash, V.K.Nandicoori. Pknb-Mediated Phosphorylation of A Novel Substrate, N-Acetylglucosamine-1-Phosphate Uridyltransferase, Modulates Its Acetyltransferase Activity. J.Mol.Biol. V. 386 451 2009.
ISSN: ISSN 0022-2836
PubMed: 19121323
DOI: 10.1016/J.JMB.2008.12.031