Magnesium in PDB 1n8w: Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis

All present enzymatic activity of Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis:
4.1.3.2;

The structure of Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis, PDB code: 1n8w was solved by C.V.Smith, C.C.Huang, A.Miczak, D.G.Russell, J.C.Sacchettini, K.Honer Zu Bentrup, Tb Structural Genomics Consortium (Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.36 / 2.70
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	120.985, 120.985, 232.787, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 28.7

The binding sites of Magnesium atom in the Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis (pdb code 1n8w). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis, PDB code: 1n8w:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Biochemical and Structural Studies of Malate Synthase 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 Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg900 b:40.5 occ:1.00 O3 A:MLT901 1.6 50.7 1.0 OE1 A:GLU434 1.9 11.4 1.0 O A:HOH1001 1.9 29.6 1.0 O4 A:MLT901 2.1 56.9 1.0 OD1 A:ASP462 2.5 9.1 1.0 C2 A:MLT901 2.7 51.9 1.0 CD A:GLU434 2.9 12.6 1.0 C4 A:MLT901 2.9 56.9 1.0 C3 A:MLT901 3.0 54.5 1.0 CG A:ASP462 3.2 9.9 1.0 OE2 A:GLU434 3.3 11.7 1.0 CB A:ASP462 3.4 10.7 1.0 C1 A:MLT901 3.9 51.2 1.0 OD1 A:ASP274 4.0 14.8 1.0 O1 A:MLT901 4.1 49.2 1.0 CG A:GLU434 4.1 12.9 1.0 O5 A:MLT901 4.2 57.1 1.0 CB A:ALA635 4.3 14.3 1.0 OD2 A:ASP462 4.3 7.9 1.0 NH1 A:ARG339 4.3 11.4 1.0 NZ A:LYS399 4.4 9.0 1.0 OE2 A:GLU273 4.4 19.6 1.0 N A:ASP462 4.4 11.5 1.0 CA A:ASP462 4.5 11.0 1.0 CB A:GLU434 4.6 12.7 1.0 CG A:ASP274 5.0 14.4 1.0

Magnesium binding site 2 out of 2 in the Biochemical and Structural Studies of Malate Synthase 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 Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1900 b:36.3 occ:1.00 O3 B:GLV1901 1.2 27.5 1.0 O B:HOH1140 2.0 19.0 1.0 C2 B:GLV1901 2.0 28.1 1.0 O1 B:GLV1901 2.1 30.0 1.0 O B:HOH1139 2.1 28.1 1.0 OD1 B:ASP462 2.3 9.1 1.0 OE2 B:GLU434 2.4 12.3 1.0 C1 B:GLV1901 2.5 26.1 1.0 CG B:ASP462 3.2 11.7 1.0 O2 B:GLV1901 3.2 28.9 1.0 CB B:ASP462 3.4 11.4 1.0 CD B:GLU434 3.7 12.3 1.0 N B:ASP462 3.8 11.6 1.0 CB B:ALA635 4.1 11.9 1.0 CA B:GLY459 4.2 13.2 1.0 CA B:ASP462 4.2 11.4 1.0 O B:GLY459 4.3 13.9 1.0 OD2 B:ASP462 4.3 13.3 1.0 OE1 B:GLU434 4.4 14.4 1.0 OD2 B:ASP274 4.4 16.3 1.0 C B:GLY459 4.4 13.5 1.0 CB B:GLU434 4.6 9.7 1.0 CE B:MET432 4.6 16.3 1.0 CG B:GLU434 4.7 10.1 1.0 CB B:LEU461 4.8 12.2 1.0 NH1 B:ARG339 4.9 15.1 1.0 N B:LEU461 4.9 12.1 1.0 C B:LEU461 5.0 11.8 1.0

C.V.Smith, C.C.Huang, A.Miczak, D.G.Russell, J.C.Sacchettini, K.Honer Zu Bentrup. Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis J.Biol.Chem. V. 278 1735 2003.
ISSN: ISSN 0021-9258
PubMed: 12393860
DOI: 10.1074/JBC.M209248200