Magnesium in PDB 3fr6: Tetramerization and Cooperativity in Plasmodium Falciparum Glutathione Transferase Are Mediated By the Atypic Loop 113-118

All present enzymatic activity of Tetramerization and Cooperativity in Plasmodium Falciparum Glutathione Transferase Are Mediated By the Atypic Loop 113-118:
2.5.1.18;

The structure of Tetramerization and Cooperativity in Plasmodium Falciparum Glutathione Transferase Are Mediated By the Atypic Loop 113-118, PDB code: 3fr6 was solved by M.Perbandt, E.Liebau, G.Ricci, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	60.612, 86.840, 74.750, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 30.2

The binding sites of Magnesium atom in the Tetramerization and Cooperativity in Plasmodium Falciparum Glutathione Transferase Are Mediated By the Atypic Loop 113-118 (pdb code 3fr6). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Tetramerization and Cooperativity in Plasmodium Falciparum Glutathione Transferase Are Mediated By the Atypic Loop 113-118, PDB code: 3fr6:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Tetramerization and Cooperativity in Plasmodium Falciparum Glutathione Transferase Are Mediated By the Atypic Loop 113-118


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Tetramerization and Cooperativity in Plasmodium Falciparum Glutathione Transferase Are Mediated By the Atypic Loop 113-118 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg212 b:47.8 occ:1.00 NE2 A:GLN71 2.7 54.4 1.0 CG A:GLN73 3.5 48.5 1.0 OG A:SER72 3.6 48.2 1.0 CD A:GLN73 3.6 53.2 1.0 O A:HOH216 3.7 35.9 1.0 N A:GLN73 3.8 45.7 1.0 OE1 A:GLN73 3.8 55.6 1.0 N A:SER72 3.9 45.1 1.0 CD A:GLN71 4.0 52.0 1.0 CB A:GLN73 4.1 46.5 1.0 NE2 A:GLN73 4.2 51.8 1.0 C A:GLN71 4.2 45.8 1.0 CA A:GLN71 4.3 46.6 1.0 CB A:GLN71 4.4 46.9 1.0 CA A:GLN73 4.6 46.0 1.0 NZ A:LYS15 4.6 47.2 1.0 CA A:SER72 4.6 46.0 1.0 C A:SER72 4.7 45.8 1.0 CB A:SER72 4.7 46.3 1.0 CG A:GLN71 4.8 48.2 1.0 OE1 A:GLN71 4.9 53.6 1.0 O A:GLN71 4.9 45.5 1.0 CE A:LYS15 5.0 47.7 1.0

Magnesium binding site 2 out of 2 in the Tetramerization and Cooperativity in Plasmodium Falciparum Glutathione Transferase Are Mediated By the Atypic Loop 113-118


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Tetramerization and Cooperativity in Plasmodium Falciparum Glutathione Transferase Are Mediated By the Atypic Loop 113-118 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg212 b:58.1 occ:1.00 O B:HOH214 3.3 36.1 1.0 NZ B:LYS15 3.4 52.1 1.0 CG B:GLN73 3.5 49.8 1.0 OG B:SER72 3.5 52.2 1.0 OE1 B:GLN73 3.6 54.1 1.0 N B:GLN73 3.7 48.8 1.0 N B:SER72 3.8 50.9 1.0 NE2 B:GLN71 4.0 58.6 1.0 CD B:GLN73 4.0 52.9 1.0 C B:GLN71 4.3 52.0 1.0 CA B:SER72 4.4 50.5 1.0 C B:SER72 4.5 49.5 1.0 CB B:GLN73 4.5 47.9 1.0 CA B:GLN71 4.5 52.9 1.0 CB B:SER72 4.5 50.5 1.0 CB B:GLN71 4.6 53.5 1.0 CE B:LYS15 4.6 51.4 1.0 CA B:GLN73 4.6 48.0 1.0 CD B:GLN71 4.8 59.9 1.0 CD B:LYS15 4.9 51.9 1.0

M.Perbandt, E.Liebau, G.Ricci. Tetramerization and Cooperativity in Plasmodium Falciparum Glutathione Transferase Are Mediated By the Atypic Loop 113-118 To Be Published.