Magnesium in PDB 3t2g: Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Y229F Variant with Dhap

All present enzymatic activity of Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Y229F Variant with Dhap:
3.1.3.11; 4.1.2.13;

The structure of Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Y229F Variant with Dhap, PDB code: 3t2g 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)	47.72 / 3.00
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	112.430, 112.430, 151.520, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 23.4

The binding sites of Magnesium atom in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Y229F Variant with Dhap (pdb code 3t2g). 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, Y229F Variant with Dhap, PDB code: 3t2g:
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, Y229F Variant with Dhap


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, Y229F Variant with Dhap within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg408 b:13.2 occ:1.00 OD2 A:ASP234 2.0 54.9 1.0 OD1 A:ASP52 2.0 39.2 1.0 O2P A:13P410 2.0 74.9 1.0 OD1 A:ASP132 2.4 33.6 1.0 OD2 A:ASP53 2.7 43.1 1.0 OD1 A:ASP53 2.8 41.2 1.0 P A:13P410 2.9 74.7 1.0 CG A:ASP53 3.0 41.1 1.0 CG A:ASP52 3.1 37.9 1.0 CG A:ASP234 3.2 53.0 1.0 O3P A:13P410 3.3 72.5 1.0 O1P A:13P410 3.4 74.9 1.0 CG A:ASP132 3.5 32.7 1.0 OD2 A:ASP11 3.6 45.2 1.0 OD2 A:ASP52 3.6 37.6 1.0 OD2 A:ASP132 3.9 32.6 1.0 OD1 A:ASP234 4.0 53.0 1.0 CB A:ASP234 4.2 52.9 1.0 NZ A:LYS133 4.2 29.8 1.0 C A:ASP52 4.3 38.0 1.0 CG A:ASP11 4.3 41.1 1.0 O1 A:13P410 4.3 73.5 1.0 N A:ASP53 4.3 38.3 1.0 CB A:ASP11 4.3 38.4 1.0 CB A:ASP52 4.4 37.2 1.0 CB A:ASP53 4.4 39.2 1.0 N A:ASP52 4.5 36.5 1.0 MG A:MG409 4.5 51.0 1.0 CA A:ASP52 4.6 37.3 1.0 O A:ASP52 4.6 38.3 1.0 N A:LYS133 4.6 31.1 1.0 CB A:ASP132 4.7 31.1 1.0 CA A:ASP53 4.8 38.9 1.0 CE A:LYS133 4.9 31.7 1.0 CA A:ASP132 5.0 31.4 1.0

Magnesium binding site 2 out of 2 in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Y229F Variant with Dhap


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, Y229F Variant with Dhap within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg409 b:51.0 occ:1.00 OD2 A:ASP11 2.2 45.2 1.0 OD2 A:ASP52 2.3 37.6 1.0 ND1 A:HIS18 2.4 40.7 1.0 O3P A:13P410 2.4 72.5 1.0 OE1 A:GLN95 2.8 51.8 1.0 CE1 A:HIS18 2.9 41.2 1.0 CG A:ASP11 3.2 41.1 1.0 CG A:ASP52 3.4 37.9 1.0 CG A:HIS18 3.5 39.0 1.0 OD1 A:ASP11 3.6 44.5 1.0 CD A:GLN95 3.7 52.0 1.0 P A:13P410 3.7 74.7 1.0 NE2 A:GLN95 3.9 51.8 1.0 OD1 A:ASP52 4.0 39.2 1.0 NE2 A:HIS18 4.1 41.5 1.0 O2P A:13P410 4.1 74.9 1.0 CB A:HIS18 4.1 37.4 1.0 O1 A:13P410 4.2 73.5 1.0 CD2 A:HIS18 4.4 40.3 1.0 CA A:HIS18 4.4 37.3 1.0 CB A:ASP52 4.5 37.2 1.0 MG A:MG408 4.5 13.2 1.0 CB A:ASP11 4.5 38.4 1.0 C1 A:13P410 4.6 70.5 1.0 O A:GLY17 4.9 36.8 1.0 O A:TYR91 4.9 41.4 1.0 CG A:GLN95 5.0 51.4 1.0 NZ A:LYS133 5.0 29.8 1.0 O1P A:13P410 5.0 74.9 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