Magnesium in PDB 3t2b: Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Ligand Free

All present enzymatic activity of Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Ligand Free:
3.1.3.11; 4.1.2.13;

The structure of Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Ligand Free, PDB code: 3t2b was solved by J.Du, R.Say, W.Lue, G.Fuchs, O.Einsle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.79 / 1.52
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	112.532, 112.532, 151.126, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 18.8

The binding sites of Magnesium atom in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Ligand Free (pdb code 3t2b). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Ligand Free, PDB code: 3t2b:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Ligand Free


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Ligand Free within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg408 b:12.9 occ:1.00 OD2 A:ASP52 2.0 11.9 1.0 O A:HOH416 2.1 17.7 1.0 O A:HOH417 2.1 15.7 1.0 OD2 A:ASP11 2.1 15.0 1.0 O A:HOH415 2.2 17.8 1.0 ND1 A:HIS18 2.3 14.7 1.0 CG A:ASP52 3.1 8.7 1.0 CE1 A:HIS18 3.1 15.9 1.0 CG A:ASP11 3.2 16.1 1.0 CG A:HIS18 3.4 13.0 1.0 OD1 A:ASP11 3.4 15.7 1.0 CB A:HIS18 3.7 11.5 1.0 OD1 A:ASP52 3.9 10.2 1.0 CB A:ASP52 4.0 10.3 1.0 O A:HOH427 4.0 13.4 1.0 O A:HOH426 4.0 10.2 1.0 O A:HOH480 4.1 29.6 1.0 CA A:HIS18 4.2 12.0 1.0 O A:HOH624 4.3 32.5 1.0 NE2 A:HIS18 4.3 15.9 1.0 O A:HOH622 4.4 23.3 1.0 O A:HOH623 4.4 35.6 1.0 CD2 A:HIS18 4.4 14.7 1.0 CB A:ASP11 4.5 14.0 1.0 MG A:MG409 4.7 10.5 1.0 O A:GLY17 4.8 14.7 1.0 O A:TYR91 4.9 17.9 1.0

Magnesium binding site 2 out of 2 in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Ligand Free


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Ligand Free within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg409 b:10.5 occ:1.00 OD2 A:ASP234 1.9 16.1 1.0 OD1 A:ASP52 2.0 10.2 1.0 OD1 A:ASP132 2.0 11.1 1.0 O A:HOH426 2.1 10.2 1.0 OD2 A:ASP53 2.1 15.2 1.0 O A:HOH427 2.1 13.4 1.0 CG A:ASP53 3.1 20.2 1.0 CG A:ASP234 3.1 15.0 1.0 CG A:ASP52 3.1 8.7 1.0 CG A:ASP132 3.1 8.9 1.0 OD1 A:ASP53 3.4 14.9 1.0 OD2 A:ASP52 3.5 11.9 1.0 NZ A:LYS133 3.7 8.4 1.0 OD2 A:ASP132 3.7 10.7 1.0 OD1 A:ASP234 4.0 17.1 1.0 CB A:ASP234 4.0 11.4 1.0 O A:HOH425 4.0 14.5 1.0 O A:HOH428 4.0 24.1 1.0 O A:HOH417 4.1 15.7 1.0 OD2 A:ASP11 4.1 15.0 1.0 N A:LYS133 4.3 8.2 1.0 CB A:ASP132 4.3 10.1 1.0 CB A:ASP53 4.3 13.5 1.0 N A:ASP53 4.4 12.0 1.0 C A:ASP52 4.4 13.2 1.0 CB A:ASP52 4.5 10.3 1.0 N A:ASP52 4.5 10.4 1.0 CA A:ASP132 4.5 9.1 1.0 CA A:ASP52 4.7 12.0 1.0 MG A:MG408 4.7 12.9 1.0 CD A:LYS133 4.9 8.6 1.0 CA A:ASP53 4.9 11.8 1.0 O A:ASP52 4.9 13.6 1.0 CE A:LYS133 4.9 10.3 1.0 C A:ASP132 4.9 10.7 1.0 CG A:ASP11 5.0 16.1 1.0

J.Du, R.F.Say, W.Lu, G.Fuchs, O.Einsle. Active-Site Remodelling in the Bifunctional Fructose-1,6-Bisphosphate Aldolase/Phosphatase. Nature V. 478 534 2011.
ISSN: ISSN 0028-0836
PubMed: 21983965
DOI: 10.1038/NATURE10458