Magnesium in PDB 3t2c: Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Dhap-Bound Form

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

The structure of Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Dhap-Bound Form, PDB code: 3t2c 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)	17.34 / 1.30
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	112.348, 112.348, 150.915, 90.00, 90.00, 90.00
R / Rfree (%)	10.8 / 12.9

The binding sites of Magnesium atom in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Dhap-Bound Form (pdb code 3t2c). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Dhap-Bound Form, PDB code: 3t2c:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Dhap-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, Dhap-Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg408 b:7.8 occ:0.60 O A:HOH415 2.1 14.2 1.0 O A:HOH416 2.1 10.4 0.6 O2P A:13P411 2.1 8.5 0.6 O A:LYS232 2.1 7.0 0.6 OD2 A:ASP234 2.1 8.7 1.0 O A:HOH414 2.2 9.2 1.0 O1P A:13P411 2.2 19.0 0.4 P A:13P411 3.0 15.1 0.4 CG A:ASP234 3.1 7.8 1.0 P A:13P411 3.2 8.2 0.6 C A:LYS232 3.2 6.5 0.6 MG A:MG409 3.2 7.2 1.0 O2P A:13P411 3.3 12.6 0.4 O3P A:13P411 3.4 7.5 0.6 N A:LYS232 3.4 7.6 0.6 O A:HOH736 3.5 11.6 0.4 O3P A:13P411 3.6 14.5 0.4 O A:HOH737 3.6 23.4 0.4 O1P A:13P411 3.7 7.7 0.6 NE2 A:GLN95 3.8 17.7 0.4 CA A:LYS232 3.8 7.2 0.6 CB A:ASP234 3.9 7.8 1.0 OD1 A:ASP53 3.9 9.6 1.0 OD1 A:ASP234 3.9 9.2 1.0 C A:GLY231 4.2 9.4 0.6 CD1 A:LEU222 4.2 18.2 0.6 C A:ASP233 4.3 10.1 1.0 N A:ASP233 4.3 7.3 0.6 CB A:LYS232 4.3 8.1 0.6 O A:ASP233 4.3 13.9 1.0 OD1 A:ASP96 4.3 15.8 1.0 OD2 A:ASP53 4.3 9.4 1.0 OD2 A:ASP96 4.4 13.9 1.0 OD2 A:ASP11 4.4 8.9 1.0 O1 A:13P411 4.4 19.6 0.4 CA A:GLY231 4.4 7.7 0.6 CG A:ASP53 4.5 9.8 1.0 CA A:ASP233 4.5 15.8 0.4 O1 A:13P411 4.6 9.8 0.6 CA A:ASP233 4.6 10.7 0.6 NE2 A:GLN95 4.6 10.4 0.6 N A:ASP234 4.7 10.4 1.0 CG A:ASP96 4.8 15.9 1.0 OD1 A:ASP132 4.8 7.8 1.0 NZ A:LYS9 4.8 10.1 1.0 CB A:ASP11 4.8 8.9 1.0 OD1 A:ASP52 4.9 7.9 1.0 CA A:ASP234 4.9 9.0 1.0 CD A:GLN95 5.0 15.3 0.4

Magnesium binding site 2 out of 3 in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Dhap-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, Dhap-Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg409 b:7.2 occ:1.00 O3P A:13P411 2.0 7.5 0.6 O2P A:13P411 2.0 12.6 0.4 OD1 A:ASP132 2.0 7.8 1.0 OD2 A:ASP53 2.0 9.4 1.0 OD1 A:ASP52 2.1 7.9 1.0 OD2 A:ASP234 2.1 8.7 1.0 O A:HOH414 2.1 9.2 1.0 CG A:ASP53 3.0 9.8 1.0 CG A:ASP234 3.1 7.8 1.0 CG A:ASP132 3.1 6.9 1.0 P A:13P411 3.2 8.2 0.6 CG A:ASP52 3.2 7.8 1.0 P A:13P411 3.2 15.1 0.4 MG A:MG408 3.2 7.8 0.6 OD1 A:ASP53 3.4 9.6 1.0 O2P A:13P411 3.5 8.5 0.6 OD2 A:ASP132 3.6 7.3 1.0 OD2 A:ASP52 3.7 8.6 1.0 NZ A:LYS133 3.7 7.4 1.0 OD1 A:ASP234 3.8 9.2 1.0 O1P A:13P411 3.8 19.0 0.4 CB A:ASP234 3.9 7.8 1.0 O1P A:13P411 3.9 7.7 0.6 O3P A:13P411 3.9 14.5 0.4 OD2 A:ASP11 4.0 8.9 1.0 O A:HOH736 4.1 11.6 0.4 CB A:ASP132 4.3 6.4 1.0 O A:HOH415 4.3 14.2 1.0 O1 A:13P411 4.3 9.8 0.6 CB A:ASP53 4.3 9.6 1.0 N A:ASP53 4.4 6.9 1.0 C A:ASP52 4.4 7.2 1.0 O1 A:13P411 4.4 19.6 0.4 N A:LYS133 4.5 5.6 1.0 CB A:ASP52 4.5 7.9 1.0 N A:ASP52 4.5 7.0 1.0 MG A:MG410 4.6 8.4 1.0 CA A:ASP132 4.6 5.9 1.0 CA A:ASP52 4.7 7.2 1.0 O A:HOH416 4.8 10.4 0.6 CE A:LYS133 4.8 7.1 1.0 CG A:ASP11 4.8 8.0 1.0 O A:LYS232 4.9 7.0 0.6 CB A:ASP11 4.9 8.9 1.0 CA A:ASP53 4.9 7.7 1.0 O A:ASP52 4.9 8.8 1.0 CD A:LYS133 4.9 7.4 1.0

Magnesium binding site 3 out of 3 in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Dhap-Bound Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Dhap-Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg410 b:8.4 occ:1.00 O1P A:13P411 2.0 7.7 0.6 OD2 A:ASP52 2.1 8.6 1.0 OD2 A:ASP11 2.1 8.9 1.0 O3P A:13P411 2.1 14.5 0.4 O A:HOH413 2.1 9.8 1.0 OE1 A:GLN95 2.2 10.2 0.6 OE1 A:GLN95 2.2 10.3 0.4 ND1 A:HIS18 2.2 8.9 1.0 CG A:ASP52 3.1 7.8 1.0 CE1 A:HIS18 3.1 9.4 1.0 CG A:ASP11 3.1 8.0 1.0 CD A:GLN95 3.1 12.4 0.6 CD A:GLN95 3.2 15.3 0.4 P A:13P411 3.3 8.2 0.6 CG A:HIS18 3.3 8.1 1.0 P A:13P411 3.4 15.1 0.4 NE2 A:GLN95 3.4 10.4 0.6 OD1 A:ASP11 3.5 9.3 1.0 NE2 A:GLN95 3.5 17.7 0.4 CB A:HIS18 3.7 7.4 1.0 OD1 A:ASP52 3.8 7.9 1.0 O3P A:13P411 3.8 7.5 0.6 O2P A:13P411 3.8 12.6 0.4 O A:HOH414 3.9 9.2 1.0 CB A:ASP52 4.0 7.9 1.0 O1 A:13P411 4.1 9.8 0.6 O1 A:13P411 4.2 19.6 0.4 CA A:HIS18 4.2 7.6 1.0 NE2 A:HIS18 4.3 9.9 1.0 O2P A:13P411 4.3 8.5 0.6 CB A:ASP11 4.4 8.9 1.0 CD2 A:HIS18 4.4 10.2 1.0 CG A:GLN95 4.5 14.3 0.6 CG A:GLN95 4.5 14.7 0.4 O1P A:13P411 4.5 19.0 0.4 MG A:MG409 4.6 7.2 1.0 C1 A:13P411 4.6 9.1 0.6 O A:HOH416 4.7 10.4 0.6 CB A:GLN95 4.8 13.3 0.6 C1 A:13P411 4.8 21.2 0.4 CB A:GLN95 4.9 13.8 0.4 NZ A:LYS133 5.0 7.4 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