Magnesium in PDB 4rji: Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I

All present enzymatic activity of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I:
4.1.3.18;

The structure of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I, PDB code: 4rji was solved by B.Sommer, H.Von Moeller, M.Haack, F.Qoura, C.Langner, G.Bourenkov, D.Garbe, T.Brueck, B.Loll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.66 / 3.20
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	140.647, 140.647, 238.877, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 25.3

The binding sites of Magnesium atom in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I (pdb code 4rji). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I, PDB code: 4rji:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1001 b:96.0 occ:1.00 O2A A:TPP1000 1.8 0.5 1.0 O3B A:TPP1000 1.9 0.1 1.0 OD1 A:ASP451 2.1 86.9 1.0 OD1 A:ASP478 2.2 0.6 1.0 O A:THR480 2.6 82.6 1.0 PA A:TPP1000 3.1 0.6 1.0 CG A:ASP451 3.1 89.8 1.0 PB A:TPP1000 3.2 0.2 1.0 CG A:ASP478 3.2 0.9 1.0 O3A A:TPP1000 3.4 0.7 1.0 OD2 A:ASP451 3.5 92.8 1.0 OD2 A:ASP478 3.6 0.5 1.0 C A:THR480 3.8 83.3 1.0 N A:ASP451 3.9 90.2 1.0 O7 A:TPP1000 4.1 0.1 1.0 O A:TRP476 4.1 89.0 1.0 O1A A:TPP1000 4.1 1.0 1.0 O2B A:TPP1000 4.1 0.9 1.0 O1B A:TPP1000 4.2 0.6 1.0 N A:THR480 4.3 89.9 1.0 N A:GLY452 4.3 97.7 1.0 CB A:ASP451 4.4 87.1 1.0 CB A:ASP478 4.5 1.0 1.0 CE1 A:TYR547 4.5 0.4 1.0 CA A:GLY450 4.6 0.3 1.0 N A:ASP482 4.6 0.0 1.0 N A:ASP478 4.6 0.7 1.0 CA A:THR480 4.6 84.6 1.0 CA A:ASP451 4.7 86.3 1.0 C A:GLY450 4.7 0.1 1.0 N A:SER479 4.8 0.0 1.0 N A:TYR481 4.8 95.9 1.0 CA A:TYR481 5.0 94.6 1.0 C A:ASP451 5.0 85.5 1.0

Magnesium binding site 2 out of 4 in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg602 b:63.9 occ:1.00 O2A B:TPP601 1.9 86.0 1.0 O3B B:TPP601 2.1 94.5 1.0 OD1 B:ASP478 2.3 91.4 1.0 OD1 B:ASP451 2.3 71.6 1.0 O B:THR480 2.9 0.9 1.0 PA B:TPP601 3.1 80.3 1.0 CG B:ASP451 3.1 71.6 1.0 PB B:TPP601 3.1 87.8 1.0 O3A B:TPP601 3.2 83.0 1.0 CG B:ASP478 3.3 91.2 1.0 N B:ASP451 3.5 62.0 1.0 OD2 B:ASP451 3.5 72.6 1.0 O B:TRP476 3.7 63.7 1.0 OD2 B:ASP478 3.8 96.3 1.0 O2B B:TPP601 3.9 85.1 1.0 O1A B:TPP601 4.0 79.4 1.0 C B:THR480 4.1 0.9 1.0 N B:GLY452 4.2 1.0 1.0 O7 B:TPP601 4.2 86.2 1.0 CA B:GLY450 4.2 75.8 1.0 CB B:ASP451 4.3 65.3 1.0 C B:GLY450 4.3 76.9 1.0 O1B B:TPP601 4.4 86.7 1.0 CA B:ASP451 4.4 62.0 1.0 N B:ASP478 4.4 86.7 1.0 N B:THR480 4.4 0.0 1.0 CB B:ASP478 4.5 85.7 1.0 CE1 B:TYR547 4.6 92.6 1.0 N B:SER479 4.7 97.6 1.0 OH B:TYR547 4.8 85.9 1.0 C B:ASP451 4.8 68.0 1.0 CA B:THR480 4.9 0.7 1.0 C B:TRP476 4.9 64.2 1.0 CA B:ASP478 4.9 89.5 1.0 N B:ASP482 4.9 0.6 1.0

Magnesium binding site 3 out of 4 in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg1001 b:43.0 occ:1.00 O C:THR480 2.0 61.8 1.0 OD1 C:ASP478 2.1 75.2 1.0 OD1 C:ASP451 2.2 72.9 1.0 O2A C:TPP1000 2.3 79.0 1.0 O3B C:TPP1000 2.5 77.3 1.0 O C:HOH1104 2.5 28.7 1.0 C C:THR480 3.1 64.5 1.0 CG C:ASP451 3.1 72.1 1.0 CG C:ASP478 3.2 74.5 1.0 N C:THR480 3.4 64.3 1.0 OD2 C:ASP451 3.5 72.2 1.0 PA C:TPP1000 3.6 77.0 1.0 OD2 C:ASP478 3.6 70.7 1.0 PB C:TPP1000 3.7 75.2 1.0 CA C:THR480 3.8 63.9 1.0 O3A C:TPP1000 3.9 81.2 1.0 CZ C:PHE500 4.0 66.1 1.0 N C:SER479 4.2 86.2 1.0 N C:ASP451 4.2 69.7 1.0 N C:TYR481 4.2 71.7 1.0 N C:GLY452 4.3 63.3 1.0 O7 C:TPP1000 4.3 72.8 1.0 C C:SER479 4.4 86.8 1.0 CB C:ASP451 4.5 70.2 1.0 CB C:ASP478 4.5 73.1 1.0 N C:ASP482 4.5 79.0 1.0 OG1 C:THR480 4.5 61.4 1.0 CA C:TYR481 4.6 71.3 1.0 N C:ASP478 4.6 68.1 1.0 O1B C:TPP1000 4.6 72.8 1.0 CA C:SER479 4.7 89.1 1.0 O C:TRP476 4.7 54.6 1.0 O1A C:TPP1000 4.7 69.5 1.0 C C:ASP478 4.7 75.7 1.0 CE2 C:PHE500 4.7 65.6 1.0 O2B C:TPP1000 4.7 70.5 1.0 CA C:ASP451 4.7 68.9 1.0 CB C:THR480 4.8 62.0 1.0 CA C:ASP478 4.8 71.5 1.0 CE1 C:PHE500 4.9 65.9 1.0 C C:ASP451 4.9 70.1 1.0

Magnesium binding site 4 out of 4 in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form I within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg1001 b:34.2 occ:1.00 OD1 D:ASP478 2.0 63.5 1.0 O2A D:TPP1000 2.1 50.6 1.0 OD1 D:ASP451 2.4 53.6 1.0 O3B D:TPP1000 2.5 50.5 1.0 O D:THR480 2.7 47.1 1.0 CG D:ASP478 2.9 58.6 1.0 CG D:ASP451 3.2 54.5 1.0 OD2 D:ASP478 3.4 55.0 1.0 PA D:TPP1000 3.4 54.6 1.0 PB D:TPP1000 3.5 50.5 1.0 O3A D:TPP1000 3.5 53.2 1.0 OD2 D:ASP451 3.6 57.0 1.0 N D:ASP451 3.8 48.8 1.0 O D:TRP476 3.9 53.7 1.0 C D:THR480 3.9 48.4 1.0 O2B D:TPP1000 4.0 48.9 1.0 CB D:ASP478 4.1 57.5 1.0 N D:THR480 4.3 53.3 1.0 CE1 D:TYR547 4.3 51.7 1.0 N D:ASP478 4.3 58.1 1.0 O1A D:TPP1000 4.4 51.1 1.0 O7 D:TPP1000 4.4 50.2 1.0 N D:GLY452 4.4 56.4 1.0 CA D:GLY450 4.4 62.1 1.0 CB D:ASP451 4.4 50.5 1.0 N D:ASP482 4.6 62.0 1.0 C D:GLY450 4.6 62.8 1.0 N D:SER479 4.6 74.7 1.0 CA D:ASP451 4.6 48.5 1.0 CA D:THR480 4.7 52.4 1.0 CA D:ASP478 4.7 57.2 1.0 O1B D:TPP1000 4.8 49.5 1.0 OH D:TYR547 4.8 48.9 1.0 N D:TYR481 4.9 48.5 1.0 C D:ASP478 4.9 60.7 1.0 CB D:ASP482 5.0 62.7 1.0 C D:TRP476 5.0 52.8 1.0

B.Sommer, H.Von Moeller, M.Haack, F.Qoura, C.Langner, G.Bourenkov, D.Garbe, B.Loll, T.Brueck. Detailed Structure-Function Correlations of Bacillus Subtilis Acetolactate Synthase To Be Published.