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Magnesium in PDB 4x33: Structure of the Elongator Cofactor Complex KTI11/KTI13 at 1.45A

Protein crystallography data

The structure of Structure of the Elongator Cofactor Complex KTI11/KTI13 at 1.45A, PDB code: 4x33 was solved by O.Kolaj-Robin, A.G.Mcewen, J.Cavarelli, B.Seraphin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.23 / 1.45
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 49.790, 89.009, 163.530, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 17.6

Other elements in 4x33:

The structure of Structure of the Elongator Cofactor Complex KTI11/KTI13 at 1.45A also contains other interesting chemical elements:

Iron (Fe) 1 atom
Chlorine (Cl) 8 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Elongator Cofactor Complex KTI11/KTI13 at 1.45A (pdb code 4x33). 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 Structure of the Elongator Cofactor Complex KTI11/KTI13 at 1.45A, PDB code: 4x33:

Magnesium binding site 1 out of 1 in 4x33

Go back to Magnesium Binding Sites List in 4x33
Magnesium binding site 1 out of 1 in the Structure of the Elongator Cofactor Complex KTI11/KTI13 at 1.45A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Elongator Cofactor Complex KTI11/KTI13 at 1.45A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg407

b:61.7
occ:1.00
O B:HOH658 2.1 69.7 1.0
O B:HOH647 2.3 58.5 1.0
O B:HOH672 2.4 54.5 1.0
O B:HOH568 2.6 46.1 1.0
HE1 B:HIS203 3.3 32.3 1.0
O B:HOH553 4.0 25.3 1.0
O B:HOH878 4.2 49.3 1.0
O B:HOH525 4.3 26.8 1.0
CE1 B:HIS203 4.4 30.9 1.0
OE2 B:GLU162 4.4 56.1 1.0
HG3 B:GLU162 4.5 30.5 1.0
O B:HOH875 4.7 39.8 1.0

Reference:

O.Kolaj-Robin, A.G.Mcewen, J.Cavarelli, B.Seraphin. Structure of the Elongator Cofactor Complex KTI11/KTI13 Provides Insight Into the Role of KTI13 in Elongator-Dependent Trna Modification. Febs J. 2015.
ISSN: ISSN 1742-464X
PubMed: 25604895
DOI: 10.1111/FEBS.13199
Page generated: Tue Aug 20 14:03:20 2024

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