Magnesium in PDB 6i2p: Crystal Structure of the Mycobacterium Tuberculosis Pknb Kinase Domain (L33E Mutant) in Complex with Its Substrate Gara

All present enzymatic activity of Crystal Structure of the Mycobacterium Tuberculosis Pknb Kinase Domain (L33E Mutant) in Complex with Its Substrate Gara:
2.7.11.1;

The structure of Crystal Structure of the Mycobacterium Tuberculosis Pknb Kinase Domain (L33E Mutant) in Complex with Its Substrate Gara, PDB code: 6i2p was solved by G.Andre-Leroux, V.Hindie, N.Barilone, M.Bellinzoni, P.M.Alzari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.85 / 2.37
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.310, 70.460, 188.600, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 23.4

The binding sites of Magnesium atom in the Crystal Structure of the Mycobacterium Tuberculosis Pknb Kinase Domain (L33E Mutant) in Complex with Its Substrate Gara (pdb code 6i2p). 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 the Mycobacterium Tuberculosis Pknb Kinase Domain (L33E Mutant) in Complex with Its Substrate Gara, PDB code: 6i2p:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Mycobacterium Tuberculosis Pknb Kinase Domain (L33E Mutant) in Complex with Its Substrate Gara


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 the Mycobacterium Tuberculosis Pknb Kinase Domain (L33E Mutant) in Complex with Its Substrate Gara within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:84.1 occ:1.00 O2G A:ACP301 2.5 70.2 1.0 O2B A:ACP301 2.6 66.5 1.0 OD1 A:ASP156 3.0 62.9 1.0 OE2 A:GLU59 3.4 82.7 1.0 PG A:ACP301 3.8 70.0 1.0 PB A:ACP301 3.8 64.6 1.0 CG A:ASP156 3.8 61.1 1.0 CD A:GLU59 3.9 86.1 1.0 OD2 A:ASP156 4.1 64.7 1.0 O1P A:TPO173 4.2 79.9 1.0 C3B A:ACP301 4.2 67.3 1.0 NZ A:LYS40 4.2 59.0 1.0 OE1 A:GLU59 4.3 76.2 1.0 O1B A:ACP301 4.4 63.6 1.0 O1G A:ACP301 4.6 70.5 1.0 CG A:GLU59 4.8 59.1 1.0 O3G A:ACP301 4.9 71.1 1.0 CB A:ASP156 5.0 50.2 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Mycobacterium Tuberculosis Pknb Kinase Domain (L33E Mutant) in Complex with Its Substrate Gara


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 the Mycobacterium Tuberculosis Pknb Kinase Domain (L33E Mutant) in Complex with Its Substrate Gara within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:78.1 occ:1.00 OD1 B:ASP156 2.3 80.3 1.0 O2B B:ACP301 2.7 65.6 1.0 O2G B:ACP301 3.0 73.1 1.0 CG B:ASP156 3.3 76.0 1.0 OE2 B:GLU59 3.7 0.1 1.0 OD2 B:ASP156 3.8 81.6 1.0 PG B:ACP301 4.0 74.2 1.0 PB B:ACP301 4.0 64.0 1.0 O3G B:ACP301 4.0 75.3 1.0 NZ B:LYS40 4.2 69.2 1.0 CD B:GLU59 4.3 0.3 1.0 C3B B:ACP301 4.4 68.4 1.0 CB B:ASP156 4.5 55.3 1.0 O1B B:ACP301 4.7 64.3 1.0 OE1 B:GLU59 4.8 0.8 1.0

T.Wagner, G.Andre-Leroux, V.Hindie, N.Barilone, M.N.Lisa, S.Hoos, B.Raynal, B.Vulliez-Le Normand, H.M.O'hare, M.Bellinzoni, P.M.Alzari. Structural Insights Into the Functional Versatility of An Fha Domain Protein in Mycobacterial Signaling. Sci.Signal. V. 12 2019.
ISSN: ESSN 1937-9145
PubMed: 31064884
DOI: 10.1126/SCISIGNAL.AAV9504