Magnesium in PDB 4ch4: Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Crotonyl Lysine

All present enzymatic activity of Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Crotonyl Lysine:
6.1.1.26;

The structure of Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Crotonyl Lysine, PDB code: 4ch4 was solved by V.Fluegel, M.Vrabel, S.Schneider, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.42 / 2.16
Space group	P 64
Cell size a, b, c (Å), α, β, γ (°)	105.045, 105.045, 71.771, 90.00, 90.00, 120.00
R / Rfree (%)	16.536 / 20.88

The binding sites of Magnesium atom in the Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Crotonyl Lysine (pdb code 4ch4). 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 Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Crotonyl Lysine, PDB code: 4ch4:

Magnesium binding site 1 out of 1 in the Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Crotonyl Lysine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Crotonyl Lysine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1455 b:70.0 occ:1.00 OE2 A:GLU396 2.6 39.5 1.0 OAI A:YLC500 2.7 63.0 1.0 OE1 A:GLU396 3.4 46.5 1.0 CD A:GLU396 3.4 42.2 1.0 PBN A:YLC500 3.5 61.5 1.0 OAF A:YLC500 3.7 61.7 1.0 CB A:SER399 3.8 39.6 1.0 O5' A:YLC500 4.0 59.2 1.0 OG A:SER399 4.1 45.9 1.0 C5' A:YLC500 4.6 59.0 1.0 O3' A:YLC500 4.7 57.5 1.0 CG A:GLU396 4.9 39.3 1.0 C3' A:YLC500 4.9 56.9 1.0 CA A:SER399 5.0 37.6 1.0

V.Flugel, M.Vrabel, S.Schneider. Structural Basis For the Site-Specific Incorporation of Lysine Derivatives Into Proteins. Plos One V. 9E96198 2014.
ISSN: ISSN 1932-6203
PubMed: 24760130
DOI: 10.1371/JOURNAL.PONE.0096198