Magnesium in PDB 1eqr: Crystal Structure of Free Aspartyl-Trna Synthetase From Escherichia Coli

All present enzymatic activity of Crystal Structure of Free Aspartyl-Trna Synthetase From Escherichia Coli:
6.1.1.12;

The structure of Crystal Structure of Free Aspartyl-Trna Synthetase From Escherichia Coli, PDB code: 1eqr was solved by B.Rees, G.Webster, M.Delarue, M.Boeglin, D.Moras, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.70
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	117.749, 161.958, 131.599, 90.00, 110.36, 90.00
R / Rfree (%)	19.8 / 26.9

The binding sites of Magnesium atom in the Crystal Structure of Free Aspartyl-Trna Synthetase From Escherichia Coli (pdb code 1eqr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Free Aspartyl-Trna Synthetase From Escherichia Coli, PDB code: 1eqr:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Free Aspartyl-Trna Synthetase From Escherichia Coli


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 Free Aspartyl-Trna Synthetase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg901 b:2.9 occ:1.00 O A:HOH1042 2.0 2.9 1.0 OE2 A:GLU482 2.1 54.7 1.0 O A:HOH1043 2.4 62.6 1.0 OE1 A:GLU482 2.4 53.5 1.0 CD A:GLU482 2.6 51.8 1.0 O A:HOH1046 2.8 51.2 1.0 CG A:GLU482 4.2 44.2 1.0 OD2 A:ASP475 4.6 23.5 1.0 O A:HOH1045 4.9 41.5 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Free Aspartyl-Trna Synthetase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Free Aspartyl-Trna Synthetase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg902 b:2.9 occ:1.00 O B:HOH1030 1.8 2.9 1.0 OE2 B:GLU482 2.1 23.0 1.0 OE1 B:GLU482 2.2 35.9 1.0 O B:HOH1031 2.2 42.8 1.0 CD B:GLU482 2.4 27.8 1.0 CG B:GLU482 4.0 17.4 1.0 OD2 B:ASP475 4.4 26.9 1.0 CB B:GLU482 4.7 21.0 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Free Aspartyl-Trna Synthetase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Free Aspartyl-Trna Synthetase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg903 b:2.9 occ:1.00 O C:HOH1042 1.7 6.2 1.0 O C:HOH1041 2.0 2.9 1.0 OE1 C:GLU482 2.1 27.1 1.0 O C:HOH1039 2.2 38.2 1.0 OE2 C:GLU482 2.5 23.4 1.0 CD C:GLU482 2.6 23.5 1.0 CG C:GLU482 4.2 14.4 1.0 OD2 C:ASP475 4.4 33.3 1.0 O C:HOH1043 4.5 48.4 1.0 O C:HOH1044 4.6 20.8 1.0 CB C:GLU482 4.9 20.5 1.0

B.Rees, G.Webster, M.Delarue, M.Boeglin, D.Moras. Aspartyl Trna-Synthetase From Escherichia Coli: Flexibility and Adaptability to the Substrates. J.Mol.Biol. V. 299 1157 2000.
ISSN: ISSN 0022-2836
PubMed: 10873442
DOI: 10.1006/JMBI.2000.3792