Magnesium in PDB 5kwa: Complete Structure of the Mycobacterium Tuberculosis Proteasomal Atpase Mpa

The structure of Complete Structure of the Mycobacterium Tuberculosis Proteasomal Atpase Mpa, PDB code: 5kwa was solved by T.Wang, Y.J.Wu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.45 / 2.90
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	111.931, 111.931, 196.072, 90.00, 90.00, 120.00
R / Rfree (%)	22.8 / 26.9

The binding sites of Magnesium atom in the Complete Structure of the Mycobacterium Tuberculosis Proteasomal Atpase Mpa (pdb code 5kwa). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Complete Structure of the Mycobacterium Tuberculosis Proteasomal Atpase Mpa, PDB code: 5kwa:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Complete Structure of the Mycobacterium Tuberculosis Proteasomal Atpase Mpa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Complete Structure of the Mycobacterium Tuberculosis Proteasomal Atpase Mpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg702 b:32.6 occ:1.00 O1B A:ADP701 2.2 33.6 1.0 OG1 A:THR300 2.2 33.4 1.0 O A:HOH808 2.2 40.1 1.0 O1A A:ADP701 2.3 36.6 1.0 PB A:ADP701 3.4 34.6 1.0 CB A:THR300 3.4 33.5 1.0 PA A:ADP701 3.6 35.4 1.0 O3A A:ADP701 3.8 35.7 1.0 O3B A:ADP701 3.9 34.6 1.0 O A:HOH806 4.0 45.1 1.0 OD2 A:ASP371 4.0 42.3 1.0 CG2 A:THR300 4.2 33.6 1.0 OD1 A:ASP371 4.2 41.5 1.0 O5' A:ADP701 4.5 36.5 1.0 CG A:ASP371 4.5 42.0 1.0 CA A:THR300 4.6 33.8 1.0 N A:THR300 4.6 33.2 1.0 O2A A:ADP701 4.7 35.0 1.0 O2B A:ADP701 4.7 32.9 1.0 OE2 A:GLU372 4.9 49.9 1.0

Magnesium binding site 2 out of 2 in the Complete Structure of the Mycobacterium Tuberculosis Proteasomal Atpase Mpa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Complete Structure of the Mycobacterium Tuberculosis Proteasomal Atpase Mpa within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg702 b:33.5 occ:1.00 OG1 B:THR300 2.2 35.6 1.0 O1B B:ADP701 2.2 40.2 1.0 O B:HOH801 2.2 40.3 1.0 O1A B:ADP701 2.4 41.3 1.0 PB B:ADP701 3.4 41.8 1.0 CB B:THR300 3.5 35.9 1.0 PA B:ADP701 3.7 39.0 1.0 O2B B:ADP701 3.7 40.4 1.0 OD2 B:ASP371 4.0 47.2 1.0 O3A B:ADP701 4.0 40.6 1.0 OD1 B:ASP371 4.0 46.9 1.0 CG2 B:THR300 4.2 36.7 1.0 O5' B:ADP701 4.2 39.1 1.0 CG B:ASP371 4.4 46.0 1.0 CA B:THR300 4.6 35.1 1.0 N B:THR300 4.6 35.9 1.0 O3B B:ADP701 4.7 43.9 1.0 O2A B:ADP701 4.9 40.4 1.0 OE2 B:GLU372 5.0 63.8 1.0 CG B:GLU372 5.0 60.2 1.0

Y.Wu, K.Hu, D.Li, L.Bai, S.Yang, J.B.Jastrab, S.Xiao, Y.Hu, S.Zhang, K.H.Darwin, T.Wang, H.Li. Mycobacterium Tuberculosis Proteasomal Atpase Mpa Has A Beta-Grasp Domain That Hinders Docking with the Proteasome Core Protease Mol. Microbiol. V. 105 227 2017.
ISSN: ESSN 1365-2958
PubMed: 28419599
DOI: 10.1111/MMI.13695