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Magnesium in PDB 1j09: Crystal Structure of Thermus Thermophilus Glutamyl-Trna Synthetase Complexed with Atp and Glu

Enzymatic activity of Crystal Structure of Thermus Thermophilus Glutamyl-Trna Synthetase Complexed with Atp and Glu

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

Protein crystallography data

The structure of Crystal Structure of Thermus Thermophilus Glutamyl-Trna Synthetase Complexed with Atp and Glu, PDB code: 1j09 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) 37.12 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 81.920, 82.620, 83.110, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 22.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Thermus Thermophilus Glutamyl-Trna Synthetase Complexed with Atp and Glu (pdb code 1j09). 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 and Glu, PDB code: 1j09:

Magnesium binding site 1 out of 1 in 1j09

Go back to Magnesium Binding Sites List in 1j09
Magnesium binding site 1 out of 1 in the Crystal Structure of Thermus Thermophilus Glutamyl-Trna Synthetase Complexed with Atp and Glu


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 and Glu within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:20.4
occ:1.00
 O A:HOH1395 2.0 19.7 1.0
O A:HOH1397 2.0 24.5 1.0
O A:HOH1396 2.0 22.3 1.0
O1A A:ATP501 2.0 21.9 1.0
O1B A:ATP501 2.1 22.0 1.0
O1G A:ATP501 2.1 25.0 1.0
PB A:ATP501 3.2 21.3 1.0
PA A:ATP501 3.3 21.0 1.0
PG A:ATP501 3.3 24.4 1.0
O3B A:ATP501 3.5 23.9 1.0
O3A A:ATP501 3.7 22.3 1.0
O5' A:ATP501 3.8 22.0 1.0
O A:HOH1270 4.0 45.3 1.0
OE2 A:GLU208 4.2 21.1 1.0
O A:HOH1162 4.2 35.7 1.0
O2G A:ATP501 4.3 24.2 1.0
OE1 A:GLU208 4.3 22.8 1.0
NZ A:LYS243 4.3 21.4 1.0
O3G A:ATP501 4.3 27.2 1.0
O A:HOH1138 4.5 36.1 1.0
C8 A:ATP501 4.5 20.6 1.0
O2B A:ATP501 4.5 21.7 1.0
O2A A:ATP501 4.6 23.0 1.0
CE A:LYS243 4.6 25.7 1.0
CD A:GLU208 4.7 21.5 1.0
O A:HOH1085 4.7 27.0 1.0

Reference:

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
Page generated: Mon Dec 14 06:07:11 2020

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