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Magnesium in PDB 1exm: Crystal Structure of Thermus Thermophilus Elongation Factor Tu (Ef-Tu) in Complex with the Gtp Analogue Gppnhp.

Protein crystallography data

The structure of Crystal Structure of Thermus Thermophilus Elongation Factor Tu (Ef-Tu) in Complex with the Gtp Analogue Gppnhp., PDB code: 1exm was solved by T.Hogg, J.R.Mesters, R.Hilgenfeld, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.78 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 150.500, 99.500, 40.200, 90.00, 95.30, 90.00
R / Rfree (%) 20.9 / 24.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Thermus Thermophilus Elongation Factor Tu (Ef-Tu) in Complex with the Gtp Analogue Gppnhp. (pdb code 1exm). 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 Crystal Structure of Thermus Thermophilus Elongation Factor Tu (Ef-Tu) in Complex with the Gtp Analogue Gppnhp., PDB code: 1exm:

Magnesium binding site 1 out of 1 in 1exm

Go back to Magnesium Binding Sites List in 1exm
Magnesium binding site 1 out of 1 in the Crystal Structure of Thermus Thermophilus Elongation Factor Tu (Ef-Tu) in Complex with the Gtp Analogue Gppnhp.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Thermus Thermophilus Elongation Factor Tu (Ef-Tu) in Complex with the Gtp Analogue Gppnhp. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg407

b:19.4
occ:1.00
O1G A:GNP406 1.9 16.0 1.0
OG1 A:THR62 2.1 10.6 1.0
OG1 A:THR25 2.1 11.9 1.0
O2B A:GNP406 2.1 13.4 1.0
O A:HOH414 2.2 13.1 1.0
O A:HOH417 2.3 14.8 1.0
CB A:THR62 3.1 12.8 1.0
PG A:GNP406 3.1 14.3 1.0
PB A:GNP406 3.2 14.2 1.0
CB A:THR25 3.2 15.7 1.0
N3B A:GNP406 3.3 16.0 1.0
O3G A:GNP406 3.7 20.1 1.0
N A:THR25 3.8 15.7 1.0
OD2 A:ASP51 4.0 20.9 1.0
CA A:THR25 4.1 15.8 1.0
CG2 A:THR62 4.1 14.3 1.0
CA A:THR62 4.2 15.6 1.0
N A:THR62 4.2 17.5 1.0
O2G A:GNP406 4.2 15.1 1.0
O2A A:GNP406 4.2 19.9 1.0
O3A A:GNP406 4.2 17.4 1.0
OD2 A:ASP81 4.2 17.6 1.0
OD1 A:ASP51 4.2 14.7 1.0
O1B A:GNP406 4.3 11.2 1.0
CG2 A:THR25 4.3 12.5 1.0
O A:CYS82 4.6 15.9 1.0
CG A:ASP51 4.6 18.6 1.0
PA A:GNP406 4.6 17.8 1.0
OD1 A:ASP81 4.7 14.9 1.0
CB A:LYS24 4.7 16.2 1.0
CE A:LYS24 4.7 13.7 1.0
O1A A:GNP406 4.8 14.5 1.0
C A:LYS24 4.8 15.2 1.0
CG A:ASP81 4.9 17.2 1.0

Reference:

R.Hilgenfeld, J.R.Mesters, T.Hogg. Insights Into the Gtpase Mechanism of Ef-Tu From Structural Studies The Ribosome: Structure, V. 28 347 2000FUNCTION, Antibiotics, Andcellular Interactions.
Page generated: Sat Aug 9 20:49:40 2025

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