Magnesium in PDB 1n75: Crystal Structure of Thermus Thermophilus Glutamyl-Trna Synthetase Complexed with Atp.

All present enzymatic activity of Crystal Structure of Thermus Thermophilus Glutamyl-Trna Synthetase Complexed with Atp.:
6.1.1.17;

The structure of Crystal Structure of Thermus Thermophilus Glutamyl-Trna Synthetase Complexed with Atp., PDB code: 1n75 was solved by S.Sekine, O.Nureki, D.Y.Dubois, S.Bernier, R.Chenevert, J.Lapointe, D.G.Vassylyev, S.Yokoyama, Riken Structuralgenomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.54 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	82.715, 84.062, 83.447, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 23.6

The binding sites of Magnesium atom in the Crystal Structure of Thermus Thermophilus Glutamyl-Trna Synthetase Complexed with Atp. (pdb code 1n75). 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 Glutamyl-Trna Synthetase Complexed with Atp., PDB code: 1n75:

Magnesium binding site 1 out of 1 in the Crystal Structure of Thermus Thermophilus Glutamyl-Trna Synthetase Complexed with Atp.


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 Glutamyl-Trna Synthetase Complexed with Atp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:31.2 occ:1.00 O1G A:ATP501 2.0 29.1 1.0 O1B A:ATP501 2.0 27.2 1.0 O A:HOH1357 2.0 28.5 1.0 O A:HOH1356 2.1 31.2 1.0 O A:HOH1355 2.1 25.1 1.0 O1A A:ATP501 2.1 32.1 1.0 PB A:ATP501 3.2 29.1 1.0 PG A:ATP501 3.3 33.2 1.0 PA A:ATP501 3.4 32.2 1.0 O3B A:ATP501 3.5 30.1 1.0 O3A A:ATP501 3.7 31.4 1.0 O5' A:ATP501 4.0 33.2 1.0 O2G A:ATP501 4.1 30.4 1.0 NZ A:LYS243 4.2 27.4 1.0 O A:HOH1210 4.2 37.8 1.0 OE1 A:GLU208 4.3 36.0 1.0 O3G A:ATP501 4.3 30.9 1.0 O A:HOH1088 4.4 31.6 1.0 OE2 A:GLU208 4.4 36.5 1.0 C8 A:ATP501 4.5 30.9 1.0 O2B A:ATP501 4.5 28.1 1.0 CE A:LYS243 4.5 29.8 1.0 O2A A:ATP501 4.6 32.6 1.0 CD A:GLU208 4.8 35.4 1.0 N7 A:ATP501 4.9 28.0 1.0

S.Sekine, O.Nureki, D.Y.Dubois, S.Bernier, R.Chenevert, J.Lapointe, D.G.Vassylyev, S.Yokoyama. Atp Binding By Glutamyl-Trna Synthetase Is Switched to the Productive Mode By Trna Binding Embo J. V. 22 676 2003.
ISSN: ISSN 0261-4189
PubMed: 12554668
DOI: 10.1093/EMBOJ/CDG053