Magnesium in PDB 2cv0: Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and L-Glutamate

All present enzymatic activity of Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and L-Glutamate:
6.1.1.17;

The structure of Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and L-Glutamate, PDB code: 2cv0 was solved by S.Sekine, S.Yokoyama, Riken Structural Genomics/Proteomicsinitiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 2.40
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	110.727, 219.321, 135.400, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 27.1

The binding sites of Magnesium atom in the Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and L-Glutamate (pdb code 2cv0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and L-Glutamate, PDB code: 2cv0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and L-Glutamate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and L-Glutamate within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg901 b:40.9 occ:1.00 O C:HOH1150 2.7 40.2 1.0 O C:HOH1075 3.2 41.9 1.0 O2 C:C509 3.5 48.0 1.0 OP2 C:A546 3.6 48.8 1.0 N7 C:A546 3.6 44.2 1.0 N7 C:A545 3.7 41.0 1.0 C8 C:A545 3.9 41.7 1.0 N3 C:C509 4.2 50.2 1.0 C8 C:A546 4.2 47.3 1.0 C2 C:C509 4.3 50.2 1.0 C5 C:A545 4.4 34.4 1.0 C5 C:A546 4.5 46.2 1.0 N9 C:A545 4.7 43.7 1.0 O C:HOH1132 4.7 37.2 1.0 N6 C:A546 4.7 32.1 1.0 C3' C:A545 4.8 51.0 1.0 P C:A546 4.9 50.8 1.0 OP2 C:G522 4.9 37.0 1.0

Magnesium binding site 2 out of 2 in the Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and L-Glutamate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and L-Glutamate within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg902 b:58.0 occ:1.00 O2 D:C509 3.6 53.6 1.0 N7 D:A546 3.6 40.3 1.0 N7 D:A545 3.6 42.1 1.0 C8 D:A545 3.9 46.7 1.0 OP2 D:A546 4.0 39.1 1.0 N3 D:C509 4.1 41.7 1.0 C8 D:A546 4.2 38.5 1.0 O D:HOH1036 4.2 40.8 1.0 C2 D:C509 4.3 51.7 1.0 C5 D:A545 4.4 45.4 1.0 C5 D:A546 4.5 48.9 1.0 OP2 D:G522 4.7 37.3 1.0 N9 D:A545 4.8 54.7 1.0 N6 D:A546 4.8 41.1 1.0

S.Sekine, M.Shichiri, S.Bernier, R.Chenevert, J.Lapointe, S.Yokoyama. Structural Bases of Transfer Rna-Dependent Amino Acid Recognition and Activation By Glutamyl-Trna Synthetase Structure V. 14 1791 2006.
ISSN: ISSN 0969-2126
PubMed: 17161369
DOI: 10.1016/J.STR.2006.10.005