Magnesium in PDB 2vhw: Crystal Structure of Holo L-Alanine Dehydrogenase From Mycobacterium Tuberculosis in the Open and Closed Conformation

All present enzymatic activity of Crystal Structure of Holo L-Alanine Dehydrogenase From Mycobacterium Tuberculosis in the Open and Closed Conformation:
1.4.1.1;

The structure of Crystal Structure of Holo L-Alanine Dehydrogenase From Mycobacterium Tuberculosis in the Open and Closed Conformation, PDB code: 2vhw was solved by D.Agren, G.Schneider, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.0
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	177.028, 172.015, 98.556, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 21.2

The binding sites of Magnesium atom in the Crystal Structure of Holo L-Alanine Dehydrogenase From Mycobacterium Tuberculosis in the Open and Closed Conformation (pdb code 2vhw). 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 Holo L-Alanine Dehydrogenase From Mycobacterium Tuberculosis in the Open and Closed Conformation, PDB code: 2vhw:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Holo L-Alanine Dehydrogenase From Mycobacterium Tuberculosis in the Open and Closed Conformation


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 Holo L-Alanine Dehydrogenase From Mycobacterium Tuberculosis in the Open and Closed Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1372 b:48.4 occ:1.00 O A:HOH2192 2.0 46.0 1.0 NE2 A:HIS327 2.3 40.7 1.0 O A:HOH2190 2.4 50.1 1.0 O A:HOH2191 2.7 44.8 1.0 CD2 A:HIS327 3.1 42.2 1.0 OE2 A:GLU323 3.1 52.3 1.0 CE1 A:HIS327 3.3 43.1 1.0 OE1 A:GLU323 3.7 53.3 1.0 CD A:GLU323 3.8 50.6 1.0 OD2 A:ASP326 4.3 44.3 1.0 CG A:HIS327 4.3 41.9 1.0 ND1 A:HIS327 4.4 42.4 1.0 CB A:ASP326 4.5 42.7 1.0 CG A:ASP326 4.9 43.9 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Holo L-Alanine Dehydrogenase From Mycobacterium Tuberculosis in the Open and Closed Conformation


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 Holo L-Alanine Dehydrogenase From Mycobacterium Tuberculosis in the Open and Closed Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1371 b:45.9 occ:1.00 O B:HOH2014 2.0 44.7 1.0 O B:HOH2274 2.0 31.2 1.0 O B:HOH2277 2.2 35.4 1.0 O B:HOH2279 2.2 42.3 1.0 NE2 B:HIS327 2.2 33.5 1.0 CE1 B:HIS327 3.1 35.7 1.0 CD2 B:HIS327 3.3 34.3 1.0 OE1 B:GLU323 3.8 33.2 0.3 OD2 B:ASP326 4.0 38.8 1.0 OE2 B:GLU323 4.1 35.4 0.3 O B:HOH2136 4.1 50.0 1.0 ND1 B:HIS327 4.3 33.9 1.0 CD B:GLU323 4.3 35.5 0.3 CG B:HIS327 4.4 34.9 1.0 CB B:ASP326 4.5 35.6 1.0 O B:HOH2036 4.7 48.8 1.0 CG B:ASP326 4.7 37.7 1.0

D.Agren, M.Stehr, C.L.Berthold, S.Kapoor, W.Oehlmann, M.Singh, G.Schneider. Three-Dimensional Structures of Apo- and Holo-L- Alanine Dehydrogenase From Mycobacterium Tuberculosis Reveal Conformational Changes Upon Coenzyme Binding. J.Mol.Biol. V. 377 1161 2008.
ISSN: ISSN 0022-2836
PubMed: 18304579
DOI: 10.1016/J.JMB.2008.01.091