Magnesium in PDB 6ayv: Crystal Structure of Fructose-1,6-Bisphosphatase T84A From Mycobacterium Tuberculosis

All present enzymatic activity of Crystal Structure of Fructose-1,6-Bisphosphatase T84A From Mycobacterium Tuberculosis:
3.1.3.11;

The structure of Crystal Structure of Fructose-1,6-Bisphosphatase T84A From Mycobacterium Tuberculosis, PDB code: 6ayv was solved by C.Abad-Zapatero, N.Wolf, H.J.Gutka, F.Movahedzadeh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.77 / 2.30
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	131.240, 131.240, 144.149, 90.00, 90.00, 120.00
R / Rfree (%)	19 / 24.7

The binding sites of Magnesium atom in the Crystal Structure of Fructose-1,6-Bisphosphatase T84A From Mycobacterium Tuberculosis (pdb code 6ayv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Fructose-1,6-Bisphosphatase T84A From Mycobacterium Tuberculosis, PDB code: 6ayv:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Fructose-1,6-Bisphosphatase T84A 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 Crystal Structure of Fructose-1,6-Bisphosphatase T84A From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:62.0 occ:1.00 OD1 A:ASP82 2.4 49.0 1.0 OD2 A:ASP79 2.5 56.0 1.0 O A:HOH587 2.7 64.7 1.0 OE2 A:GLU208 2.8 54.4 1.0 CG A:ASP79 3.3 50.5 1.0 CA A:ASP82 3.4 51.6 1.0 CG A:ASP82 3.4 52.5 1.0 OD1 A:ASP79 3.4 51.3 1.0 CG A:GLU208 3.5 43.6 1.0 CD A:GLU208 3.6 53.8 1.0 C1 A:F6P401 3.6 55.4 1.0 O1 A:F6P401 3.7 60.8 1.0 N A:GLY83 3.8 57.4 1.0 CB A:ASP82 3.8 47.8 1.0 C A:ASP82 3.9 54.9 1.0 O A:ILE81 3.9 47.5 1.0 O A:HOH617 4.0 66.7 1.0 C3 A:F6P401 4.0 50.9 1.0 O A:HOH557 4.1 61.3 1.0 O3 A:F6P401 4.2 45.8 1.0 O A:HOH514 4.2 64.4 1.0 O A:HOH603 4.3 61.6 1.0 C2 A:F6P401 4.4 52.5 1.0 N A:ASP82 4.4 49.6 1.0 OD2 A:ASP82 4.5 51.5 1.0 C A:ILE81 4.6 46.1 1.0 CB A:ASP79 4.8 46.4 1.0 O A:HOH561 4.8 58.2 1.0 OE1 A:GLU208 4.8 52.9 1.0 O A:ASP82 4.8 46.9 1.0 CA A:GLY83 4.9 52.9 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Fructose-1,6-Bisphosphatase T84A 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 Crystal Structure of Fructose-1,6-Bisphosphatase T84A From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg406 b:65.2 occ:1.00 O A:ARG192 2.0 67.5 1.0 O A:HOH510 2.6 68.1 1.0 O A:THR197 2.6 51.1 1.0 O A:ALA190 2.6 59.2 1.0 OG A:SER195 2.6 65.1 1.0 O A:SER189 2.8 54.3 1.0 C A:ARG192 3.2 65.3 1.0 C A:ALA190 3.2 52.6 1.0 CB A:SER195 3.5 70.9 1.0 O A:PRO193 3.7 94.2 1.0 N A:ARG192 3.7 55.5 1.0 CA A:ALA190 3.8 47.6 1.0 C A:THR197 3.8 52.5 1.0 O A:HOH594 3.8 70.4 1.0 C A:SER189 3.9 52.5 1.0 C A:CYS191 3.9 61.1 1.0 N A:CYS191 4.0 51.1 1.0 CA A:ARG192 4.0 63.8 1.0 C A:PRO193 4.0 81.3 1.0 N A:PRO193 4.1 74.0 1.0 CA A:PRO193 4.2 77.0 1.0 O A:HOH529 4.2 47.4 1.0 N A:SER195 4.3 73.3 1.0 N A:ALA190 4.3 49.4 1.0 CG A:ARG192 4.4 71.2 1.0 O A:CYS191 4.4 59.2 1.0 CA A:CYS191 4.4 54.2 1.0 CA A:SER195 4.5 71.0 1.0 N A:THR197 4.5 55.5 1.0 CA A:THR197 4.7 59.4 1.0 CA A:ASP198 4.7 56.0 1.0 N A:ASP198 4.7 56.4 1.0 CB A:ARG192 4.8 62.5 1.0 N A:HIS194 4.8 70.4 1.0 CB A:THR197 5.0 57.9 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Fructose-1,6-Bisphosphatase T84A From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Fructose-1,6-Bisphosphatase T84A From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:59.8 occ:1.00 OD2 B:ASP79 2.4 55.5 1.0 OE2 B:GLU208 2.6 54.0 1.0 OD1 B:ASP82 2.6 51.3 1.0 O B:HOH605 3.0 57.9 1.0 CG B:ASP79 3.3 54.7 1.0 CA B:ASP82 3.4 53.0 1.0 CD B:GLU208 3.4 57.8 1.0 CG B:GLU208 3.4 45.3 1.0 OD1 B:ASP79 3.5 57.5 1.0 O1 B:F6P401 3.5 69.2 1.0 CG B:ASP82 3.6 59.9 1.0 C1 B:F6P401 3.8 56.7 1.0 CB B:ASP82 3.8 48.0 1.0 C3 B:F6P401 3.9 53.4 1.0 C B:ASP82 4.0 56.3 1.0 O B:HOH579 4.0 61.2 1.0 O3 B:F6P401 4.0 50.1 1.0 O B:HOH505 4.0 52.7 1.0 N B:GLY83 4.0 58.1 1.0 O B:ILE81 4.2 50.9 1.0 C2 B:F6P401 4.4 52.3 1.0 N B:ASP82 4.4 42.3 1.0 O B:HOH652 4.5 59.8 1.0 OE1 B:GLU208 4.6 49.6 1.0 CB B:ASP79 4.7 49.3 1.0 OD2 B:ASP82 4.7 51.0 1.0 C B:ILE81 4.7 51.1 1.0 O B:ASP82 4.9 49.7 1.0 CB B:GLU208 4.9 45.0 1.0

N.M.Wolf, H.J.Gutka, F.Movahedzadeh, C.Abad-Zapatero. Structures of the Mycobacterium Tuberculosis Glpx Protein (Class II Fructose-1,6-Bisphosphatase): Implications For the Active Oligomeric State, Catalytic Mechanism and Citrate Inhibition. Acta Crystallogr D Struct V. 74 321 2018BIOL.
ISSN: ISSN 2059-7983
PubMed: 29652259
DOI: 10.1107/S2059798318002838