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Magnesium in PDB 3t2f: Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Soaked with Edta and Dhap

Enzymatic activity of Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Soaked with Edta and Dhap

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

Protein crystallography data

The structure of Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Soaked with Edta and Dhap, PDB code: 3t2f 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) 47.66 / 1.90
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 112.300, 112.300, 151.190, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 19.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Soaked with Edta and Dhap (pdb code 3t2f). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Soaked with Edta and Dhap, PDB code: 3t2f:

Magnesium binding site 1 out of 1 in 3t2f

Go back to Magnesium Binding Sites List in 3t2f
Magnesium binding site 1 out of 1 in the Fructose-1,6-Bisphosphate Aldolase/Phosphatase From Thermoproteus Neutrophilus, Soaked with Edta and 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, Soaked with Edta and Dhap within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg408

b:23.7
occ:1.00
 OD2 A:ASP234 2.2 29.0 1.0
O A:HOH476 2.2 37.4 1.0
OD1 A:ASP132 2.3 23.4 1.0
OD1 A:ASP53 2.3 25.7 1.0
OD1 A:ASP52 2.4 28.4 1.0
O A:HOH474 2.5 32.5 1.0
CG A:ASP53 3.1 27.1 1.0
OD2 A:ASP53 3.2 30.8 1.0
CG A:ASP234 3.4 27.7 1.0
CG A:ASP132 3.4 19.2 1.0
CG A:ASP52 3.5 29.3 1.0
O A:HOH475 3.6 32.3 1.0
NZ A:LYS133 3.6 21.9 1.0
OD1 A:ASP11 3.8 36.9 1.0
OD2 A:ASP132 3.9 23.8 1.0
OD2 A:ASP52 4.0 34.5 1.0
OD1 A:ASP234 4.1 32.8 1.0
O A:HOH419 4.1 25.0 1.0
N A:LYS133 4.4 16.1 1.0
CB A:ASP234 4.4 21.7 1.0
CB A:ASP53 4.5 20.3 1.0
N A:ASP53 4.5 21.0 1.0
CB A:ASP11 4.5 21.9 1.0
CG A:ASP11 4.5 31.0 1.0
C A:ASP52 4.5 22.2 1.0
CB A:ASP132 4.6 15.5 1.0
N A:ASP52 4.7 20.0 1.0
CA A:ASP132 4.8 15.2 1.0
CB A:ASP52 4.8 24.0 1.0
CE A:LYS133 4.8 20.9 1.0
O A:ASP52 4.8 23.8 1.0
CA A:ASP53 4.8 21.2 1.0
CD A:LYS133 4.9 19.9 1.0
CA A:ASP52 4.9 23.2 1.0

Reference:

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
Page generated: Mon Aug 11 03:42:14 2025

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