Magnesium in PDB 2aek: R304K Trichodiene Synthase

All present enzymatic activity of R304K Trichodiene Synthase:
4.2.3.6;

The structure of R304K Trichodiene Synthase, PDB code: 2aek was solved by L.S.Vedula, D.E.Cane, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.90
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	122.280, 122.280, 151.500, 90.00, 90.00, 120.00
R / Rfree (%)	21.3 / 25.4

The binding sites of Magnesium atom in the R304K Trichodiene Synthase (pdb code 2aek). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the R304K Trichodiene Synthase, PDB code: 2aek:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the R304K Trichodiene Synthase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of R304K Trichodiene Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg804 b:52.0 occ:1.00 OD1 A:ASP239 1.9 79.1 1.0 O A:HOH825 2.1 46.2 1.0 CG A:ASP239 2.6 77.2 1.0 O A:ILE241 2.6 49.2 1.0 OD2 A:ASP239 2.7 77.5 1.0 C A:ILE241 3.8 48.7 1.0 OE1 A:GLU233 3.8 0.9 1.0 CB A:ASP239 4.1 74.5 1.0 CB A:SER242 4.2 50.2 1.0 CD A:GLU233 4.3 99.7 1.0 OE2 A:GLU233 4.5 0.8 1.0 CA A:SER242 4.5 51.7 1.0 N A:SER242 4.6 54.4 1.0 N A:ILE241 4.9 50.1 1.0 CA A:ASP239 4.9 46.2 1.0 CA A:ILE241 4.9 50.0 1.0 CG1 A:ILE241 5.0 44.2 1.0

Magnesium binding site 2 out of 2 in the R304K Trichodiene Synthase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of R304K Trichodiene Synthase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg803 b:48.3 occ:1.00 OD1 B:ASP100 2.2 54.5 1.0 O B:HOH819 2.6 41.6 1.0 O B:ASP100 2.7 51.1 1.0 O B:HOH816 2.8 49.4 1.0 OE1 B:GLU164 2.8 96.6 1.0 O B:HOH822 2.9 57.8 1.0 O B:HOH821 3.0 57.6 1.0 O B:HOH820 3.4 52.7 1.0 CG B:ASP100 3.4 54.1 1.0 C B:ASP100 3.6 50.5 1.0 CB B:GLU164 3.7 88.4 1.0 CA B:ASP100 3.8 47.4 1.0 CD B:GLU164 3.9 97.4 1.0 CB B:ASP100 4.2 54.0 1.0 CG B:GLU164 4.2 94.2 1.0 OD2 B:ASP100 4.3 51.6 1.0 O B:HOH815 4.5 56.8 1.0 O B:CYS161 4.8 56.8 1.0 CA B:CYS161 4.8 53.9 1.0 N B:ASP101 4.9 56.1 1.0 SG B:CYS161 4.9 57.2 1.0 OE2 B:GLU164 4.9 0.0 1.0

L.S.Vedula, D.E.Cane, D.W.Christianson. Role of Arginine-304 in the Diphosphate-Triggered Active Site Closure Mechanism of Trichodiene Synthase. Biochemistry V. 44 12719 2005.
ISSN: ISSN 0006-2960
PubMed: 16171386
DOI: 10.1021/BI0510476