Magnesium in PDB 1hx9: Crystal Structure of Teas W273S Form 1

All present enzymatic activity of Crystal Structure of Teas W273S Form 1:
4.1.99.7;

The structure of Crystal Structure of Teas W273S Form 1, PDB code: 1hx9 was solved by C.S.Starks, K.A.Rising, J.Chappell, J.P.Noel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 3.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	125.820, 125.820, 122.410, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 24.7

The binding sites of Magnesium atom in the Crystal Structure of Teas W273S Form 1 (pdb code 1hx9). 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 Teas W273S Form 1, PDB code: 1hx9:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Teas W273S Form 1


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 Teas W273S Form 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg757 b:35.8 occ:1.00 OD2 A:ASP444 2.2 28.7 1.0 OE2 A:GLU452 2.3 66.5 1.0 OG1 A:THR448 2.8 38.9 1.0 O2A A:FHP900 2.8 73.6 0.8 CD A:GLU452 3.0 62.9 1.0 OE1 A:GLU452 3.3 61.7 1.0 CG A:ASP444 3.3 27.3 1.0 NH2 A:ARG441 3.6 20.3 1.0 OD1 A:ASP444 3.8 30.0 1.0 CB A:THR448 4.0 39.6 1.0 OD1 A:ASP445 4.1 33.7 1.0 O A:ASP444 4.1 27.2 1.0 PA A:FHP900 4.2 73.8 0.8 CG A:GLU452 4.3 61.0 1.0 CG2 A:THR448 4.4 40.1 1.0 C A:ASP444 4.5 25.4 1.0 CB A:ASP444 4.5 23.8 1.0 O3A A:FHP900 4.7 72.0 0.8 CZ A:ARG441 4.9 15.8 1.0 N A:ASP445 4.9 28.3 1.0 O1 A:FHP900 4.9 72.2 0.8 CA A:ASP445 5.0 28.9 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Teas W273S Form 1


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 Teas W273S Form 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg758 b:41.6 occ:1.00 OD1 A:ASP301 2.3 35.6 1.0 OD1 A:ASP305 2.3 66.7 1.0 OE1 A:GLU379 3.3 50.6 1.0 CG A:ASP305 3.4 64.1 1.0 CG A:ASP301 3.5 36.2 1.0 CD A:GLU379 3.6 47.0 1.0 OE2 A:GLU379 3.7 47.6 1.0 OD2 A:ASP305 3.9 68.0 1.0 O3A A:FHP900 3.9 72.0 0.8 CD2 A:TYR376 4.1 29.2 1.0 OD2 A:ASP301 4.2 35.3 1.0 CE2 A:TYR376 4.3 31.2 1.0 O A:ASP301 4.4 37.6 1.0 CG A:GLU379 4.6 42.8 1.0 CB A:ASP301 4.6 35.6 1.0 CB A:ASP305 4.7 58.8 1.0 CB A:PHE304 4.7 27.5 1.0 CA A:ASP301 4.8 31.8 1.0 CG A:TYR376 4.8 26.6 1.0 N A:ASP305 4.9 47.6 1.0

C.S.Starks, K.A.Rising, J.Chappell, J.P.Noel. Single Active Site Mutations Change the Specificity of A Sesquiterpene Cyclase To Be Published.