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Magnesium in PDB 4e0c: 1.8 Angstrom Resolution Crystal Structure of Transaldolase From Francisella Tularensis (Phosphate-Free)

Enzymatic activity of 1.8 Angstrom Resolution Crystal Structure of Transaldolase From Francisella Tularensis (Phosphate-Free)

All present enzymatic activity of 1.8 Angstrom Resolution Crystal Structure of Transaldolase From Francisella Tularensis (Phosphate-Free):
2.2.1.2;

Protein crystallography data

The structure of 1.8 Angstrom Resolution Crystal Structure of Transaldolase From Francisella Tularensis (Phosphate-Free), PDB code: 4e0c was solved by S.H.Light, G.Minasov, A.S.Halavaty, L.Shuvalova, L.Papazisi, W.F.Anderson, Center For Structural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.59 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.761, 87.019, 140.688, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 18.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the 1.8 Angstrom Resolution Crystal Structure of Transaldolase From Francisella Tularensis (Phosphate-Free) (pdb code 4e0c). 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 1.8 Angstrom Resolution Crystal Structure of Transaldolase From Francisella Tularensis (Phosphate-Free), PDB code: 4e0c:

Magnesium binding site 1 out of 1 in 4e0c

Go back to Magnesium Binding Sites List in 4e0c
Magnesium binding site 1 out of 1 in the 1.8 Angstrom Resolution Crystal Structure of Transaldolase From Francisella Tularensis (Phosphate-Free)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 1.8 Angstrom Resolution Crystal Structure of Transaldolase From Francisella Tularensis (Phosphate-Free) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:32.9
occ:0.75
 O A:HOH849 2.0 36.5 1.0
O A:HOH695 2.0 31.7 1.0
O A:HOH851 2.1 45.2 1.0
O A:HOH852 2.1 46.8 1.0
O A:HOH850 2.3 42.2 1.0
O A:GLU93 4.3 19.3 1.0
O A:HOH640 4.5 25.4 1.0
O A:HOH686 4.6 31.8 1.0
OE1 A:GLU93 4.8 43.9 1.0
O A:HOH855 4.9 37.2 0.5

Reference:

S.H.Light, G.Minasov, M.E.Duban, W.F.Anderson. Adherence to Burgi-Dunitz Stereochemical Principles Requires Significant Structural Rearrangements in Schiff-Base Formation: Insights From Transaldolase Complexes. Acta Crystallogr.,Sect.D V. 70 544 2014.
ISSN: ISSN 0907-4449
PubMed: 24531488
DOI: 10.1107/S1399004713030666
Page generated: Mon Aug 11 11:55:09 2025

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