Magnesium in PDB 3t2e: Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, F6P-Bound Form

All present enzymatic activity of Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, F6P-Bound Form:
3.1.3.11; 4.1.2.13;

The structure of Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, F6P-Bound Form, PDB code: 3t2e 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)	39.71 / 1.66
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	112.308, 112.308, 151.221, 90.00, 90.00, 90.00
R / Rfree (%)	15 / 17.8

The binding sites of Magnesium atom in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, F6P-Bound Form (pdb code 3t2e). 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, F6P-Bound Form, PDB code: 3t2e:
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, F6P-Bound Form


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, F6P-Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg408 b:2.2 occ:1.00 O A:HOH419 1.9 16.3 1.0 OD2 A:ASP234 2.0 17.8 1.0 OD1 A:ASP52 2.1 10.4 1.0 OD1 A:ASP132 2.1 10.8 1.0 O A:HOH418 2.1 16.2 1.0 OD2 A:ASP53 2.2 15.2 1.0 CG A:ASP53 3.0 15.7 1.0 CG A:ASP234 3.1 13.5 1.0 CG A:ASP132 3.2 7.0 1.0 CG A:ASP52 3.2 7.8 1.0 OD1 A:ASP53 3.3 19.1 1.0 OD2 A:ASP52 3.5 14.8 1.0 NZ A:LYS133 3.7 6.6 1.0 OD2 A:ASP132 3.7 8.5 1.0 O A:HOH423 3.9 15.4 1.0 OD2 A:ASP11 3.9 14.2 1.0 O A:HOH417 3.9 26.0 1.0 O A:HOH527 4.0 25.1 1.0 OD1 A:ASP234 4.0 18.6 1.0 CB A:ASP234 4.1 10.9 1.0 N A:LYS133 4.3 5.5 1.0 CB A:ASP53 4.3 8.7 1.0 CB A:ASP132 4.4 6.8 1.0 N A:ASP53 4.4 8.9 1.0 C A:ASP52 4.5 8.8 1.0 CB A:ASP52 4.5 8.3 1.0 CA A:ASP132 4.6 5.8 1.0 N A:ASP52 4.6 7.2 1.0 MG A:MG409 4.6 2.0 1.0 CA A:ASP52 4.8 9.7 1.0 CG A:ASP11 4.8 12.9 1.0 CB A:ASP11 4.8 9.6 1.0 CA A:ASP53 4.8 8.3 1.0 O A:ASP52 4.9 10.0 1.0 CE A:LYS133 4.9 7.7 1.0 CD A:LYS133 4.9 8.5 1.0

Magnesium binding site 2 out of 2 in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, F6P-Bound Form


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, F6P-Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg409 b:2.0 occ:1.00 O A:HOH416 1.9 19.4 1.0 OD2 A:ASP52 2.0 14.8 1.0 O A:HOH417 2.0 26.0 1.0 OD2 A:ASP11 2.1 14.2 1.0 ND1 A:HIS18 2.1 12.1 1.0 OE1 A:GLN95 2.4 25.9 1.0 CE1 A:HIS18 2.9 13.8 1.0 CG A:ASP11 3.0 12.9 1.0 CG A:ASP52 3.0 7.8 1.0 CG A:HIS18 3.3 10.2 1.0 OD1 A:ASP11 3.3 13.8 1.0 CD A:GLN95 3.6 38.3 1.0 CB A:HIS18 3.7 9.2 1.0 OD1 A:ASP52 3.8 10.4 1.0 O A:HOH418 3.8 16.2 1.0 CB A:ASP52 3.9 8.3 1.0 O A:HOH419 3.9 16.3 1.0 NE2 A:HIS18 4.1 11.9 1.0 NE2 A:GLN95 4.2 42.7 1.0 CA A:HIS18 4.2 7.1 1.0 CD2 A:HIS18 4.3 12.2 1.0 CB A:ASP11 4.3 9.6 1.0 O2 A:F6R3469 4.6 19.1 1.0 MG A:MG408 4.6 2.2 1.0 CG A:GLN95 4.8 36.4 1.0 O A:TYR91 5.0 13.2 1.0 NZ A:LYS133 5.0 6.6 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