Atomistry » Magnesium » PDB 4rcz-4rkf » 4rji
Atomistry »
  Magnesium »
    PDB 4rcz-4rkf »
      4rji »

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

Enzymatic activity of 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;

Protein crystallography data

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

Magnesium Binding Sites:

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 4rji

Go back to Magnesium Binding Sites List in 4rji
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 4rji

Go back to Magnesium Binding Sites List in 4rji
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 4rji

Go back to Magnesium Binding Sites List in 4rji
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 4rji

Go back to Magnesium Binding Sites List in 4rji
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

Reference:

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.
Page generated: Tue Aug 20 03:09:32 2024

Last articles

As in 4CAR
As in 4BKT
As in 4C3A
As in 4C2A
As in 4AWJ
As in 4BKS
As in 3WGH
As in 3ZPG
As in 3W88
As in 3W87
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy