Atomistry » Magnesium » PDB 2cie-2cvy » 2cv2
Atomistry »
  Magnesium »
    PDB 2cie-2cvy »
      2cv2 »

Magnesium in PDB 2cv2: Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and An Enzyme Inhibitor, Glu-Ams

Enzymatic activity of Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and An Enzyme Inhibitor, Glu-Ams

All present enzymatic activity of Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and An Enzyme Inhibitor, Glu-Ams:
6.1.1.17;

Protein crystallography data

The structure of Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and An Enzyme Inhibitor, Glu-Ams, PDB code: 2cv2 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) 46.34 / 2.69
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 110.317, 219.822, 135.831, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 26

Other elements in 2cv2:

The structure of Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and An Enzyme Inhibitor, Glu-Ams also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and An Enzyme Inhibitor, Glu-Ams (pdb code 2cv2). 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 An Enzyme Inhibitor, Glu-Ams, PDB code: 2cv2:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2cv2

Go back to Magnesium Binding Sites List in 2cv2
Magnesium binding site 1 out of 2 in the Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and An Enzyme Inhibitor, Glu-Ams


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 An Enzyme Inhibitor, Glu-Ams within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg902

b:36.5
occ:1.00
O C:HOH1340 2.8 37.3 1.0
N7 C:A546 3.6 30.7 1.0
OP2 C:A546 3.8 40.9 1.0
N7 C:A545 3.9 31.8 1.0
O2 C:C509 3.9 34.3 1.0
C8 C:A545 4.2 34.8 1.0
C8 C:A546 4.3 31.4 1.0
O C:HOH1249 4.4 38.9 1.0
N3 C:C509 4.4 31.0 1.0
OP2 C:G522 4.4 29.7 1.0
C5 C:A545 4.5 26.9 1.0
C5 C:A546 4.5 25.0 1.0
C2 C:C509 4.6 30.8 1.0
N6 C:A546 4.7 22.5 1.0
O C:HOH1133 4.9 39.4 1.0
N9 C:A545 5.0 30.3 1.0

Magnesium binding site 2 out of 2 in 2cv2

Go back to Magnesium Binding Sites List in 2cv2
Magnesium binding site 2 out of 2 in the Glutamyl-Trna Synthetase From Thermus Thermophilus in Complex with Trna(Glu) and An Enzyme Inhibitor, Glu-Ams


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 An Enzyme Inhibitor, Glu-Ams within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg901

b:33.8
occ:1.00
N7 D:A546 3.7 29.4 1.0
OP2 D:G522 4.0 32.6 1.0
O2 D:C509 4.1 33.6 1.0
N7 D:A545 4.2 33.5 1.0
OP2 D:A546 4.3 27.1 1.0
N3 D:C509 4.4 27.6 1.0
C8 D:A546 4.4 29.3 1.0
O D:HOH1097 4.5 18.8 1.0
C8 D:A545 4.6 32.9 1.0
C5 D:A546 4.6 26.7 1.0
C2 D:C509 4.7 29.0 1.0
N6 D:A546 4.8 28.3 1.0
C5 D:A545 4.9 30.2 1.0

Reference:

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
Page generated: Tue Aug 13 22:21:09 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy