Magnesium in PDB 1iq8: Crystal Structure of Archaeosine Trna-Guanine Transglycosylase From Pyrococcus Horikoshii

All present enzymatic activity of Crystal Structure of Archaeosine Trna-Guanine Transglycosylase From Pyrococcus Horikoshii:
2.4.2.29;

The structure of Crystal Structure of Archaeosine Trna-Guanine Transglycosylase From Pyrococcus Horikoshii, PDB code: 1iq8 was solved by R.Ishitani, O.Nureki, S.Fukai, T.Kijimoto, N.Nameki, M.Watanabe, H.Kondo, M.Sekine, N.Okada, S.Nishimura, 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)	50.00 / 2.20
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	99.282, 99.282, 363.740, 90.00, 90.00, 90.00
R / Rfree (%)	22.7 / 26.1

The structure of Crystal Structure of Archaeosine Trna-Guanine Transglycosylase From Pyrococcus Horikoshii also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Archaeosine Trna-Guanine Transglycosylase From Pyrococcus Horikoshii (pdb code 1iq8). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Archaeosine Trna-Guanine Transglycosylase From Pyrococcus Horikoshii, PDB code: 1iq8:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Archaeosine Trna-Guanine Transglycosylase From Pyrococcus Horikoshii


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 Archaeosine Trna-Guanine Transglycosylase From Pyrococcus Horikoshii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:26.0 occ:1.00 O A:ALA528 2.5 28.0 1.0 O A:MET566 2.6 28.1 1.0 O A:ILE567 2.6 28.0 1.0 O A:PHE569 2.6 28.1 1.0 C A:ILE567 3.3 28.5 1.0 O A:VAL531 3.3 33.2 1.0 C A:ALA528 3.4 27.7 1.0 NE2 A:GLN570 3.6 35.0 1.0 C A:MET566 3.6 27.6 1.0 CA A:ILE567 3.7 26.6 1.0 C A:PHE569 3.8 28.4 1.0 N A:ILE567 4.1 26.6 1.0 CA A:LYS529 4.1 31.2 1.0 N A:LYS529 4.2 30.0 1.0 N A:VAL568 4.2 27.5 1.0 CD A:GLN570 4.3 37.4 1.0 C A:VAL568 4.3 29.3 1.0 N A:PHE569 4.3 29.8 1.0 C A:VAL531 4.3 33.2 1.0 CA A:ALA528 4.3 28.6 1.0 CB A:VAL531 4.3 31.8 1.0 OE1 A:GLN570 4.3 38.6 1.0 CB A:ALA528 4.4 25.1 1.0 C A:LYS529 4.4 29.8 1.0 N A:VAL531 4.4 30.6 1.0 O A:LYS529 4.5 29.6 1.0 O A:VAL568 4.5 31.2 1.0 O A:HOH725 4.5 43.8 1.0 CA A:PHE569 4.6 27.8 1.0 CA A:VAL531 4.6 31.8 1.0 CA A:VAL568 4.7 30.2 1.0 N A:GLN570 4.8 29.7 1.0 CA A:MET566 4.9 28.0 1.0 CA A:GLN570 5.0 31.3 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Archaeosine Trna-Guanine Transglycosylase From Pyrococcus Horikoshii


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 Archaeosine Trna-Guanine Transglycosylase From Pyrococcus Horikoshii within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:31.9 occ:1.00 O B:ALA528 2.4 43.5 1.0 O B:ILE567 2.6 33.7 1.0 O B:MET566 2.6 35.6 1.0 O B:PHE569 2.7 38.1 1.0 O B:VAL531 3.2 36.3 1.0 C B:ALA528 3.2 43.4 1.0 C B:ILE567 3.3 34.5 1.0 NE2 B:GLN570 3.5 45.2 1.0 C B:MET566 3.7 34.2 1.0 CA B:ILE567 3.7 33.3 1.0 C B:PHE569 3.9 36.7 1.0 N B:LYS529 3.9 44.8 1.0 CA B:LYS529 3.9 46.1 1.0 CA B:ALA528 4.1 42.6 1.0 N B:ILE567 4.2 33.1 1.0 N B:PHE569 4.2 33.0 1.0 CD B:GLN570 4.2 46.3 1.0 CB B:ALA528 4.2 39.6 1.0 N B:VAL568 4.3 33.8 1.0 C B:VAL531 4.3 37.1 1.0 CB B:VAL531 4.3 38.6 1.0 OE1 B:GLN570 4.4 49.5 1.0 N B:VAL531 4.4 41.0 1.0 C B:VAL568 4.4 34.3 1.0 C B:LYS529 4.4 45.5 1.0 CA B:PHE569 4.6 35.4 1.0 CA B:VAL531 4.6 38.5 1.0 CA B:VAL568 4.7 33.7 1.0 N B:PHE530 4.8 44.3 1.0 N B:GLN570 4.9 37.9 1.0 O B:VAL568 4.9 33.5 1.0 O B:LYS529 5.0 46.9 1.0 CA B:MET566 5.0 33.0 1.0

R.Ishitani, O.Nureki, S.Fukai, T.Kijimoto, N.Nameki, M.Watanabe, H.Kondo, M.Sekine, N.Okada, S.Nishimura, S.Yokoyama. Crystal Structure of Archaeosine Trna-Guanine Transglycosylase. J.Mol.Biol. V. 318 665 2002.
ISSN: ISSN 0022-2836
PubMed: 12054814
DOI: 10.1016/S0022-2836(02)00090-6