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Magnesium in PDB 1x54: Crystal Structure of Asparaginyl-Trna Synthetase From Pyrococcus Horikoshii Complexed with Asparaginyl-Adenylate

Enzymatic activity of Crystal Structure of Asparaginyl-Trna Synthetase From Pyrococcus Horikoshii Complexed with Asparaginyl-Adenylate

All present enzymatic activity of Crystal Structure of Asparaginyl-Trna Synthetase From Pyrococcus Horikoshii Complexed with Asparaginyl-Adenylate:
6.1.1.22;

Protein crystallography data

The structure of Crystal Structure of Asparaginyl-Trna Synthetase From Pyrococcus Horikoshii Complexed with Asparaginyl-Adenylate, PDB code: 1x54 was solved by W.Iwasaki, 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) 30.29 / 1.45
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 126.071, 68.221, 75.706, 90.00, 117.18, 90.00
R / Rfree (%) 16.8 / 19.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Asparaginyl-Trna Synthetase From Pyrococcus Horikoshii Complexed with Asparaginyl-Adenylate (pdb code 1x54). 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 Asparaginyl-Trna Synthetase From Pyrococcus Horikoshii Complexed with Asparaginyl-Adenylate, PDB code: 1x54:

Magnesium binding site 1 out of 1 in 1x54

Go back to Magnesium Binding Sites List in 1x54
Magnesium binding site 1 out of 1 in the Crystal Structure of Asparaginyl-Trna Synthetase From Pyrococcus Horikoshii Complexed with Asparaginyl-Adenylate


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 Asparaginyl-Trna Synthetase From Pyrococcus Horikoshii Complexed with Asparaginyl-Adenylate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2000

b:22.6
occ:1.00
 O2P A:4AD2001 2.1 20.5 1.0
O A:HOH1702 2.1 21.7 1.0
OE1 A:GLU357 2.2 20.5 1.0
O A:HOH1705 2.2 28.8 1.0
O A:HOH1703 2.2 30.8 1.0
O A:HOH1074 2.3 27.1 1.0
CD A:GLU357 3.0 23.7 1.0
OE2 A:GLU357 3.2 28.4 1.0
P A:4AD2001 3.4 18.1 1.0
O1P A:4AD2001 3.9 18.9 1.0
O A:HOH1083 4.3 22.1 1.0
O A:HOH1060 4.4 23.5 1.0
OD1 A:ASP348 4.4 17.8 1.0
O3P A:4AD2001 4.4 18.2 1.0
O5' A:4AD2001 4.4 17.4 1.0
O3' A:4AD2001 4.4 18.2 1.0
CG A:GLU357 4.5 19.9 1.0
CA A:GLY360 4.5 12.7 1.0
C3' A:4AD2001 4.5 16.7 1.0
O A:HOH1373 4.5 40.1 1.0
OD2 A:ASP348 4.6 22.7 1.0
CG A:ASP348 4.8 17.9 1.0
O A:HOH1125 4.9 34.0 1.0
C5' A:4AD2001 5.0 16.8 1.0

Reference:

W.Iwasaki, S.Sekine, C.Kuroishi, S.Kuramitsu, M.Shirouzu, S.Yokoyama. Structural Basis of the Water-Assisted Asparagine Recognition By Asparaginyl-Trna Synthetase. J.Mol.Biol. V. 360 329 2006.
ISSN: ISSN 0022-2836
PubMed: 16753178
DOI: 10.1016/J.JMB.2006.04.068
Page generated: Tue Aug 13 17:28:10 2024

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