Magnesium in PDB 2pz8: Nad+ Synthetase From Bacillus Anthracis with Amp-Cpp and MG2+

All present enzymatic activity of Nad+ Synthetase From Bacillus Anthracis with Amp-Cpp and MG2+:
6.3.1.5;

The structure of Nad+ Synthetase From Bacillus Anthracis with Amp-Cpp and MG2+, PDB code: 2pz8 was solved by H.M.Mcdonald, P.S.Pruett, C.Deivanayagam, I.I.Protasevich, W.M.Carson, L.J.Delucas, W.J.Brouillette, C.G.Brouillette, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.00 / 2.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	107.183, 96.507, 68.633, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 22.9

The binding sites of Magnesium atom in the Nad+ Synthetase From Bacillus Anthracis with Amp-Cpp and MG2+ (pdb code 2pz8). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Nad+ Synthetase From Bacillus Anthracis with Amp-Cpp and MG2+, PDB code: 2pz8:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Nad+ Synthetase From Bacillus Anthracis with Amp-Cpp and MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Nad+ Synthetase From Bacillus Anthracis with Amp-Cpp and MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg4001 b:24.1 occ:1.00 O1G A:APC3001 2.0 23.6 1.0 O2B A:APC3001 2.1 20.6 1.0 O A:THR209 2.1 23.8 1.0 O1A A:APC3001 2.1 21.8 1.0 O A:HOH4134 2.1 21.7 1.0 O A:HOH4133 2.2 22.0 1.0 PB A:APC3001 3.0 21.1 1.0 PA A:APC3001 3.2 24.1 1.0 PG A:APC3001 3.2 24.1 1.0 C A:THR209 3.2 25.8 1.0 C3A A:APC3001 3.5 21.1 1.0 O3B A:APC3001 3.5 23.9 1.0 N A:THR209 4.0 26.1 0.0 O5' A:APC3001 4.0 21.0 1.0 N A:ALA210 4.0 24.6 1.0 CA A:ALA210 4.1 24.7 0.0 O2G A:APC3001 4.1 24.0 1.0 O A:HOH4030 4.1 25.3 1.0 O3G A:APC3001 4.1 24.4 1.0 OG A:SER47 4.2 20.0 1.0 CA A:THR209 4.2 24.9 1.0 O A:HOH4087 4.2 33.9 1.0 O1B A:APC3001 4.2 23.0 1.0 O2A A:APC3001 4.3 20.8 1.0 CG2 A:THR209 4.4 24.1 1.0 C A:ALA210 4.6 24.2 0.0 O A:HOH4059 4.6 25.5 1.0 CA A:GLY49 4.7 18.9 1.0 O A:HOH4116 4.7 31.9 1.0 O A:ALA210 4.8 24.8 1.0 CB A:SER47 4.9 17.7 1.0 CB A:THR209 4.9 25.8 1.0

Magnesium binding site 2 out of 2 in the Nad+ Synthetase From Bacillus Anthracis with Amp-Cpp and MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Nad+ Synthetase From Bacillus Anthracis with Amp-Cpp and MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg4002 b:17.9 occ:1.00 O1G B:APC3002 2.0 15.8 1.0 O2B B:APC3002 2.0 16.9 1.0 O B:THR209 2.0 16.9 1.0 O B:HOH4145 2.1 20.3 1.0 O1A B:APC3002 2.1 17.6 1.0 O B:HOH4144 2.2 20.0 1.0 PB B:APC3002 3.0 17.5 1.0 PG B:APC3002 3.1 19.0 1.0 PA B:APC3002 3.2 18.0 1.0 C B:THR209 3.2 17.7 1.0 O3B B:APC3002 3.5 16.6 1.0 C3A B:APC3002 3.6 16.7 1.0 N B:THR209 4.0 19.6 0.0 O5' B:APC3002 4.0 17.6 1.0 N B:ALA210 4.0 18.7 1.0 O2G B:APC3002 4.1 20.3 1.0 O3G B:APC3002 4.1 18.4 1.0 O B:HOH4014 4.1 15.5 1.0 CA B:ALA210 4.1 18.8 0.0 OG B:SER47 4.2 17.1 1.0 CA B:THR209 4.2 18.7 1.0 O B:HOH4067 4.2 26.7 1.0 O1B B:APC3002 4.2 17.9 1.0 O2A B:APC3002 4.3 15.6 1.0 O B:HOH4072 4.3 17.5 1.0 CG2 B:THR209 4.5 19.3 1.0 C B:ALA210 4.6 18.7 0.0 O B:HOH4036 4.6 20.6 1.0 CA B:GLY49 4.7 14.3 1.0 CB B:SER47 4.8 16.1 1.0 O B:ALA210 4.9 17.6 1.0 CB B:THR209 4.9 19.8 1.0

H.M.Mcdonald, P.S.Pruett, C.Deivanayagam, I.I.Protasevich, W.M.Carson, L.J.Delucas, W.J.Brouillette, C.G.Brouillette. Structural Adaptation of An Interacting Non-Native C-Terminal Helical Extension Revealed in the Crystal Structure of Nad(+) Synthetase From Bacillus Anthracis. Acta Crystallogr.,Sect.D V. 63 891 2007.
ISSN: ISSN 0907-4449
PubMed: 17642516
DOI: 10.1107/S0907444907029769