Magnesium in PDB 4rjj: Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II
Enzymatic activity of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II
All present enzymatic activity of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II:
4.1.3.18;
Protein crystallography data
The structure of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II, PDB code: 4rjj
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)
|
30.00 /
2.34
|
|
Space group
|
P 21 2 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
111.671,
170.003,
339.812,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
17.2 /
21.6
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II
(pdb code 4rjj). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the
Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II, PDB code: 4rjj:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 4rjj
Go back to
Magnesium Binding Sites List in 4rjj
Magnesium binding site 1 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II
 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 II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg602
b:29.7
occ:1.00
|
O
|
A:HOH861
|
2.1
|
36.0
|
1.0
|
|
OD1
|
A:ASP478
|
2.2
|
41.6
|
1.0
|
|
O
|
A:THR480
|
2.3
|
36.8
|
1.0
|
|
OD1
|
A:ASP451
|
2.3
|
33.1
|
1.0
|
|
O2A
|
A:TPP601
|
2.3
|
37.0
|
1.0
|
|
O3B
|
A:TPP601
|
2.3
|
30.6
|
1.0
|
|
CG
|
A:ASP478
|
3.3
|
37.0
|
1.0
|
|
CG
|
A:ASP451
|
3.4
|
35.3
|
1.0
|
|
C
|
A:THR480
|
3.4
|
41.6
|
1.0
|
|
PA
|
A:TPP601
|
3.5
|
38.9
|
1.0
|
|
PB
|
A:TPP601
|
3.5
|
31.9
|
1.0
|
|
N
|
A:THR480
|
3.7
|
44.7
|
1.0
|
|
OD2
|
A:ASP478
|
3.8
|
36.2
|
1.0
|
|
O3A
|
A:TPP601
|
3.8
|
38.9
|
1.0
|
|
OD2
|
A:ASP451
|
3.9
|
37.4
|
1.0
|
|
N
|
A:ASP451
|
4.0
|
27.3
|
1.0
|
|
CA
|
A:THR480
|
4.1
|
41.4
|
1.0
|
|
N
|
A:GLY452
|
4.2
|
22.1
|
1.0
|
|
O7
|
A:TPP601
|
4.2
|
37.9
|
1.0
|
|
CZ
|
A:PHE500
|
4.2
|
30.8
|
1.0
|
|
N
|
A:SER479
|
4.4
|
40.4
|
1.0
|
|
O2B
|
A:TPP601
|
4.4
|
35.3
|
1.0
|
|
CB
|
A:ASP478
|
4.4
|
26.1
|
1.0
|
|
N
|
A:ASP482
|
4.5
|
36.1
|
1.0
|
|
N
|
A:TYR481
|
4.5
|
39.4
|
1.0
|
|
O1B
|
A:TPP601
|
4.6
|
24.7
|
1.0
|
|
CB
|
A:ASP451
|
4.6
|
25.7
|
1.0
|
|
N
|
A:ASP478
|
4.6
|
31.9
|
1.0
|
|
O
|
A:TRP476
|
4.6
|
30.4
|
1.0
|
|
OG1
|
A:THR480
|
4.6
|
31.6
|
1.0
|
|
O1A
|
A:TPP601
|
4.7
|
30.6
|
1.0
|
|
CE2
|
A:TYR547
|
4.7
|
29.9
|
1.0
|
|
CA
|
A:ASP451
|
4.7
|
31.2
|
1.0
|
|
C
|
A:SER479
|
4.7
|
46.2
|
1.0
|
|
CA
|
A:TYR481
|
4.8
|
36.3
|
1.0
|
|
CA
|
A:GLY450
|
4.9
|
24.7
|
1.0
|
|
CB
|
A:ASP482
|
4.9
|
34.8
|
1.0
|
|
C
|
A:GLY450
|
4.9
|
28.9
|
1.0
|
|
CA
|
A:ASP478
|
4.9
|
39.8
|
1.0
|
|
C
|
A:ASP478
|
4.9
|
42.9
|
1.0
|
|
C
|
A:ASP451
|
4.9
|
25.2
|
1.0
|
|
CA
|
A:SER479
|
5.0
|
40.2
|
1.0
|
|
CE2
|
A:PHE500
|
5.0
|
34.5
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 4rjj
Go back to
Magnesium Binding Sites List in 4rjj
Magnesium binding site 2 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II
 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 II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg602
b:29.2
occ:1.00
|
O
|
B:HOH907
|
1.9
|
42.5
|
1.0
|
|
O2A
|
B:TPP601
|
2.1
|
31.8
|
1.0
|
|
OD1
|
B:ASP451
|
2.1
|
32.9
|
1.0
|
|
O
|
B:THR480
|
2.2
|
38.1
|
1.0
|
|
O3B
|
B:TPP601
|
2.3
|
31.7
|
1.0
|
|
OD1
|
B:ASP478
|
2.5
|
35.5
|
1.0
|
|
CG
|
B:ASP451
|
3.3
|
35.5
|
1.0
|
|
C
|
B:THR480
|
3.3
|
38.9
|
1.0
|
|
PA
|
B:TPP601
|
3.4
|
29.9
|
1.0
|
|
PB
|
B:TPP601
|
3.5
|
30.9
|
1.0
|
|
CG
|
B:ASP478
|
3.6
|
40.0
|
1.0
|
|
N
|
B:THR480
|
3.7
|
37.1
|
1.0
|
|
N
|
B:ASP451
|
3.8
|
25.5
|
1.0
|
|
O3A
|
B:TPP601
|
3.8
|
34.9
|
1.0
|
|
N
|
B:GLY452
|
3.8
|
24.2
|
1.0
|
|
OD2
|
B:ASP451
|
3.9
|
44.5
|
1.0
|
|
O7
|
B:TPP601
|
4.0
|
33.2
|
1.0
|
|
CA
|
B:THR480
|
4.1
|
40.0
|
1.0
|
|
OD2
|
B:ASP478
|
4.2
|
36.0
|
1.0
|
|
CZ
|
B:PHE500
|
4.3
|
36.7
|
1.0
|
|
N
|
B:TYR481
|
4.3
|
39.6
|
1.0
|
|
O2B
|
B:TPP601
|
4.4
|
31.2
|
1.0
|
|
CA
|
B:ASP451
|
4.4
|
24.9
|
1.0
|
|
CB
|
B:ASP451
|
4.4
|
23.8
|
1.0
|
|
N
|
B:ASP482
|
4.4
|
35.7
|
1.0
|
|
N
|
B:SER479
|
4.5
|
40.1
|
1.0
|
|
O1A
|
B:TPP601
|
4.5
|
33.0
|
1.0
|
|
CA
|
B:TYR481
|
4.6
|
32.6
|
1.0
|
|
C
|
B:ASP451
|
4.6
|
21.1
|
1.0
|
|
C
|
B:GLY450
|
4.6
|
25.6
|
1.0
|
|
O1B
|
B:TPP601
|
4.6
|
29.9
|
1.0
|
|
O
|
B:TRP476
|
4.6
|
27.2
|
1.0
|
|
CA
|
B:GLY452
|
4.7
|
27.8
|
1.0
|
|
CA
|
B:GLY450
|
4.7
|
22.0
|
1.0
|
|
C
|
B:SER479
|
4.7
|
43.2
|
1.0
|
|
CB
|
B:ASP478
|
4.8
|
37.1
|
1.0
|
|
OG1
|
B:THR480
|
4.8
|
34.2
|
1.0
|
|
N
|
B:ASP478
|
4.8
|
33.0
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 4rjj
Go back to
Magnesium Binding Sites List in 4rjj
Magnesium binding site 3 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II
 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 II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg602
b:28.6
occ:1.00
|
O2A
|
C:TPP601
|
2.1
|
29.5
|
1.0
|
|
O3B
|
C:TPP601
|
2.1
|
29.6
|
1.0
|
|
O
|
C:HOH931
|
2.2
|
32.2
|
1.0
|
|
O
|
C:THR480
|
2.2
|
35.2
|
1.0
|
|
OD1
|
C:ASP478
|
2.2
|
37.9
|
1.0
|
|
OD1
|
C:ASP451
|
2.3
|
29.5
|
1.0
|
|
CG
|
C:ASP478
|
3.3
|
38.3
|
1.0
|
|
PA
|
C:TPP601
|
3.3
|
34.9
|
1.0
|
|
C
|
C:THR480
|
3.4
|
34.6
|
1.0
|
|
PB
|
C:TPP601
|
3.4
|
27.9
|
1.0
|
|
CG
|
C:ASP451
|
3.5
|
35.9
|
1.0
|
|
O3A
|
C:TPP601
|
3.6
|
33.9
|
1.0
|
|
N
|
C:THR480
|
3.7
|
38.6
|
1.0
|
|
OD2
|
C:ASP478
|
3.9
|
34.4
|
1.0
|
|
O7
|
C:TPP601
|
4.0
|
28.7
|
1.0
|
|
N
|
C:ASP451
|
4.0
|
17.0
|
1.0
|
|
N
|
C:GLY452
|
4.1
|
18.6
|
1.0
|
|
OD2
|
C:ASP451
|
4.1
|
36.1
|
1.0
|
|
CA
|
C:THR480
|
4.1
|
38.1
|
1.0
|
|
O2B
|
C:TPP601
|
4.3
|
31.4
|
1.0
|
|
N
|
C:ASP482
|
4.3
|
34.3
|
1.0
|
|
CZ
|
C:PHE500
|
4.3
|
28.6
|
1.0
|
|
N
|
C:SER479
|
4.4
|
39.3
|
1.0
|
|
N
|
C:TYR481
|
4.4
|
33.6
|
1.0
|
|
O1B
|
C:TPP601
|
4.4
|
21.6
|
1.0
|
|
CB
|
C:ASP478
|
4.5
|
32.3
|
1.0
|
|
O1A
|
C:TPP601
|
4.6
|
29.0
|
1.0
|
|
CA
|
C:TYR481
|
4.7
|
32.3
|
1.0
|
|
N
|
C:ASP478
|
4.7
|
33.7
|
1.0
|
|
O
|
C:TRP476
|
4.7
|
25.7
|
1.0
|
|
CA
|
C:ASP451
|
4.7
|
21.6
|
1.0
|
|
CB
|
C:ASP451
|
4.7
|
19.2
|
1.0
|
|
C
|
C:SER479
|
4.7
|
36.5
|
1.0
|
|
CE2
|
C:TYR547
|
4.7
|
29.2
|
1.0
|
|
OG1
|
C:THR480
|
4.7
|
35.5
|
1.0
|
|
CA
|
C:GLY450
|
4.8
|
20.8
|
1.0
|
|
C
|
C:GLY450
|
4.8
|
22.1
|
1.0
|
|
CB
|
C:ASP482
|
4.9
|
32.3
|
1.0
|
|
C
|
C:ASP451
|
4.9
|
23.8
|
1.0
|
|
CA
|
C:GLY452
|
4.9
|
19.9
|
1.0
|
|
C
|
C:ASP478
|
5.0
|
39.0
|
1.0
|
|
CA
|
C:ASP478
|
5.0
|
36.2
|
1.0
|
|
CA
|
C:SER479
|
5.0
|
36.9
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 4rjj
Go back to
Magnesium Binding Sites List in 4rjj
Magnesium binding site 4 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II
 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 II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg602
b:25.4
occ:1.00
|
O3B
|
D:TPP601
|
2.1
|
24.1
|
1.0
|
|
O
|
D:HOH898
|
2.1
|
24.1
|
1.0
|
|
OD1
|
D:ASP478
|
2.1
|
38.5
|
1.0
|
|
OD1
|
D:ASP451
|
2.2
|
27.4
|
1.0
|
|
O
|
D:THR480
|
2.2
|
36.5
|
1.0
|
|
O2A
|
D:TPP601
|
2.3
|
23.8
|
1.0
|
|
CG
|
D:ASP478
|
3.3
|
38.0
|
1.0
|
|
PB
|
D:TPP601
|
3.4
|
24.1
|
1.0
|
|
CG
|
D:ASP451
|
3.4
|
32.3
|
1.0
|
|
C
|
D:THR480
|
3.4
|
33.5
|
1.0
|
|
PA
|
D:TPP601
|
3.5
|
28.0
|
1.0
|
|
O3A
|
D:TPP601
|
3.7
|
34.9
|
1.0
|
|
N
|
D:THR480
|
3.8
|
34.9
|
1.0
|
|
OD2
|
D:ASP478
|
3.8
|
37.0
|
1.0
|
|
OD2
|
D:ASP451
|
4.0
|
35.6
|
1.0
|
|
N
|
D:ASP451
|
4.0
|
18.6
|
1.0
|
|
O2B
|
D:TPP601
|
4.1
|
28.0
|
1.0
|
|
CA
|
D:THR480
|
4.2
|
37.4
|
1.0
|
|
O7
|
D:TPP601
|
4.2
|
34.4
|
1.0
|
|
N
|
D:GLY452
|
4.2
|
20.6
|
1.0
|
|
N
|
D:ASP482
|
4.3
|
31.1
|
1.0
|
|
N
|
D:SER479
|
4.4
|
36.3
|
1.0
|
|
CZ
|
D:PHE500
|
4.4
|
25.8
|
1.0
|
|
CB
|
D:ASP478
|
4.4
|
32.6
|
1.0
|
|
N
|
D:TYR481
|
4.5
|
25.2
|
1.0
|
|
O1B
|
D:TPP601
|
4.5
|
28.5
|
1.0
|
|
N
|
D:ASP478
|
4.6
|
35.5
|
1.0
|
|
CE2
|
D:TYR547
|
4.6
|
24.4
|
1.0
|
|
O
|
D:TRP476
|
4.6
|
24.1
|
1.0
|
|
OG1
|
D:THR480
|
4.6
|
29.9
|
1.0
|
|
CB
|
D:ASP451
|
4.6
|
14.2
|
1.0
|
|
CA
|
D:ASP451
|
4.7
|
15.9
|
1.0
|
|
O1A
|
D:TPP601
|
4.7
|
29.9
|
1.0
|
|
CA
|
D:TYR481
|
4.7
|
29.9
|
1.0
|
|
CA
|
D:GLY450
|
4.8
|
17.0
|
1.0
|
|
C
|
D:SER479
|
4.8
|
37.4
|
1.0
|
|
CB
|
D:ASP482
|
4.8
|
27.1
|
1.0
|
|
C
|
D:GLY450
|
4.8
|
20.8
|
1.0
|
|
CA
|
D:ASP478
|
4.9
|
39.4
|
1.0
|
|
C
|
D:ASP478
|
4.9
|
46.8
|
1.0
|
|
C
|
D:ASP451
|
5.0
|
22.9
|
1.0
|
|
CA
|
D:SER479
|
5.0
|
37.1
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 4rjj
Go back to
Magnesium Binding Sites List in 4rjj
Magnesium binding site 5 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg602
b:30.0
occ:1.00
|
O
|
E:HOH899
|
2.1
|
29.2
|
1.0
|
|
O3B
|
E:TPP601
|
2.2
|
30.2
|
1.0
|
|
OD1
|
E:ASP478
|
2.2
|
38.0
|
1.0
|
|
O2A
|
E:TPP601
|
2.3
|
30.7
|
1.0
|
|
OD1
|
E:ASP451
|
2.3
|
33.2
|
1.0
|
|
O
|
E:THR480
|
2.3
|
31.1
|
1.0
|
|
CG
|
E:ASP478
|
3.3
|
36.8
|
1.0
|
|
PB
|
E:TPP601
|
3.3
|
24.7
|
1.0
|
|
PA
|
E:TPP601
|
3.4
|
35.4
|
1.0
|
|
CG
|
E:ASP451
|
3.5
|
34.8
|
1.0
|
|
C
|
E:THR480
|
3.5
|
35.9
|
1.0
|
|
O3A
|
E:TPP601
|
3.6
|
35.8
|
1.0
|
|
N
|
E:THR480
|
3.8
|
34.0
|
1.0
|
|
OD2
|
E:ASP478
|
3.8
|
35.2
|
1.0
|
|
O2B
|
E:TPP601
|
4.0
|
32.9
|
1.0
|
|
N
|
E:ASP451
|
4.0
|
20.7
|
1.0
|
|
OD2
|
E:ASP451
|
4.0
|
29.9
|
1.0
|
|
O7
|
E:TPP601
|
4.2
|
34.3
|
1.0
|
|
CA
|
E:THR480
|
4.2
|
37.6
|
1.0
|
|
N
|
E:GLY452
|
4.3
|
18.3
|
1.0
|
|
CB
|
E:ASP478
|
4.4
|
30.6
|
1.0
|
|
N
|
E:ASP482
|
4.4
|
33.6
|
1.0
|
|
CE2
|
E:TYR547
|
4.4
|
27.4
|
1.0
|
|
N
|
E:SER479
|
4.5
|
36.9
|
1.0
|
|
O1B
|
E:TPP601
|
4.6
|
24.2
|
1.0
|
|
CZ
|
E:PHE500
|
4.6
|
35.0
|
1.0
|
|
OG1
|
E:THR480
|
4.6
|
36.0
|
1.0
|
|
N
|
E:TYR481
|
4.6
|
36.1
|
1.0
|
|
O
|
E:TRP476
|
4.6
|
21.1
|
1.0
|
|
O1A
|
E:TPP601
|
4.6
|
28.9
|
1.0
|
|
CB
|
E:ASP451
|
4.7
|
20.7
|
1.0
|
|
N
|
E:ASP478
|
4.7
|
30.9
|
1.0
|
|
CA
|
E:ASP451
|
4.7
|
21.8
|
1.0
|
|
CA
|
E:GLY450
|
4.8
|
19.6
|
1.0
|
|
C
|
E:GLY450
|
4.8
|
21.0
|
1.0
|
|
CA
|
E:TYR481
|
4.8
|
34.2
|
1.0
|
|
CB
|
E:ASP482
|
4.9
|
30.4
|
1.0
|
|
C
|
E:SER479
|
4.9
|
37.0
|
1.0
|
|
CA
|
E:ASP478
|
4.9
|
32.4
|
1.0
|
|
C
|
E:ASP478
|
4.9
|
34.5
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 4rjj
Go back to
Magnesium Binding Sites List in 4rjj
Magnesium binding site 6 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg602
b:24.7
occ:1.00
|
O
|
F:HOH915
|
2.0
|
32.4
|
1.0
|
|
O2A
|
F:TPP601
|
2.2
|
31.6
|
1.0
|
|
OD1
|
F:ASP451
|
2.2
|
34.2
|
1.0
|
|
O3B
|
F:TPP601
|
2.2
|
27.4
|
1.0
|
|
O
|
F:THR480
|
2.2
|
37.5
|
1.0
|
|
OD1
|
F:ASP478
|
2.3
|
36.5
|
1.0
|
|
CG
|
F:ASP451
|
3.3
|
36.0
|
1.0
|
|
C
|
F:THR480
|
3.4
|
36.6
|
1.0
|
|
PA
|
F:TPP601
|
3.4
|
33.4
|
1.0
|
|
CG
|
F:ASP478
|
3.4
|
33.5
|
1.0
|
|
PB
|
F:TPP601
|
3.5
|
30.9
|
1.0
|
|
N
|
F:THR480
|
3.7
|
35.2
|
1.0
|
|
O3A
|
F:TPP601
|
3.8
|
32.4
|
1.0
|
|
OD2
|
F:ASP451
|
3.8
|
43.4
|
1.0
|
|
N
|
F:ASP451
|
4.0
|
19.6
|
1.0
|
|
OD2
|
F:ASP478
|
4.0
|
29.6
|
1.0
|
|
N
|
F:GLY452
|
4.1
|
22.2
|
1.0
|
|
O7
|
F:TPP601
|
4.1
|
30.4
|
1.0
|
|
CA
|
F:THR480
|
4.1
|
37.5
|
1.0
|
|
N
|
F:ASP482
|
4.3
|
31.4
|
1.0
|
|
O2B
|
F:TPP601
|
4.4
|
33.5
|
1.0
|
|
CZ
|
F:PHE500
|
4.4
|
32.6
|
1.0
|
|
N
|
F:TYR481
|
4.4
|
34.6
|
1.0
|
|
N
|
F:SER479
|
4.4
|
35.2
|
1.0
|
|
O1B
|
F:TPP601
|
4.5
|
18.3
|
1.0
|
|
CB
|
F:ASP478
|
4.5
|
29.4
|
1.0
|
|
CB
|
F:ASP451
|
4.6
|
24.3
|
1.0
|
|
O1A
|
F:TPP601
|
4.6
|
29.2
|
1.0
|
|
CA
|
F:TYR481
|
4.6
|
30.9
|
1.0
|
|
CA
|
F:ASP451
|
4.6
|
18.9
|
1.0
|
|
N
|
F:ASP478
|
4.7
|
31.7
|
1.0
|
|
O
|
F:TRP476
|
4.7
|
27.2
|
1.0
|
|
C
|
F:SER479
|
4.7
|
39.0
|
1.0
|
|
OG1
|
F:THR480
|
4.7
|
29.1
|
1.0
|
|
CE2
|
F:TYR547
|
4.7
|
29.2
|
1.0
|
|
CA
|
F:GLY450
|
4.8
|
21.0
|
1.0
|
|
C
|
F:GLY450
|
4.8
|
22.3
|
1.0
|
|
C
|
F:ASP451
|
4.8
|
21.9
|
1.0
|
|
CA
|
F:GLY452
|
4.9
|
22.9
|
1.0
|
|
CB
|
F:ASP482
|
4.9
|
30.8
|
1.0
|
|
CA
|
F:SER479
|
4.9
|
39.2
|
1.0
|
|
C
|
F:ASP478
|
5.0
|
38.6
|
1.0
|
|
CA
|
F:ASP478
|
5.0
|
30.4
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 4rjj
Go back to
Magnesium Binding Sites List in 4rjj
Magnesium binding site 7 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg602
b:21.8
occ:1.00
|
OD1
|
G:ASP451
|
1.9
|
27.8
|
1.0
|
|
O2A
|
G:TPP601
|
2.2
|
31.3
|
1.0
|
|
O
|
G:THR480
|
2.3
|
30.4
|
1.0
|
|
OD1
|
G:ASP478
|
2.3
|
38.2
|
1.0
|
|
O3B
|
G:TPP601
|
2.3
|
25.2
|
1.0
|
|
O
|
G:HOH890
|
2.3
|
25.7
|
1.0
|
|
CG
|
G:ASP451
|
3.1
|
34.4
|
1.0
|
|
PA
|
G:TPP601
|
3.4
|
28.4
|
1.0
|
|
CG
|
G:ASP478
|
3.4
|
38.1
|
1.0
|
|
C
|
G:THR480
|
3.4
|
36.6
|
1.0
|
|
PB
|
G:TPP601
|
3.5
|
23.8
|
1.0
|
|
O3A
|
G:TPP601
|
3.6
|
27.2
|
1.0
|
|
N
|
G:ASP451
|
3.7
|
24.0
|
1.0
|
|
OD2
|
G:ASP451
|
3.8
|
41.0
|
1.0
|
|
N
|
G:THR480
|
3.8
|
38.3
|
1.0
|
|
OD2
|
G:ASP478
|
4.0
|
32.7
|
1.0
|
|
N
|
G:GLY452
|
4.0
|
22.2
|
1.0
|
|
O2B
|
G:TPP601
|
4.2
|
29.4
|
1.0
|
|
O7
|
G:TPP601
|
4.2
|
32.6
|
1.0
|
|
CA
|
G:THR480
|
4.2
|
34.4
|
1.0
|
|
CB
|
G:ASP451
|
4.3
|
22.3
|
1.0
|
|
CA
|
G:ASP451
|
4.4
|
21.7
|
1.0
|
|
N
|
G:SER479
|
4.4
|
36.3
|
1.0
|
|
CZ
|
G:PHE500
|
4.4
|
33.8
|
1.0
|
|
N
|
G:TYR481
|
4.5
|
33.7
|
1.0
|
|
O
|
G:TRP476
|
4.5
|
26.6
|
1.0
|
|
C
|
G:GLY450
|
4.5
|
21.2
|
1.0
|
|
N
|
G:ASP482
|
4.6
|
33.3
|
1.0
|
|
CA
|
G:GLY450
|
4.6
|
23.8
|
1.0
|
|
CB
|
G:ASP478
|
4.6
|
33.9
|
1.0
|
|
O1A
|
G:TPP601
|
4.6
|
23.7
|
1.0
|
|
N
|
G:ASP478
|
4.6
|
34.3
|
1.0
|
|
O1B
|
G:TPP601
|
4.7
|
21.0
|
1.0
|
|
C
|
G:ASP451
|
4.7
|
20.8
|
1.0
|
|
CA
|
G:TYR481
|
4.7
|
27.8
|
1.0
|
|
C
|
G:SER479
|
4.8
|
44.4
|
1.0
|
|
OG1
|
G:THR480
|
4.8
|
33.2
|
1.0
|
|
CE2
|
G:TYR547
|
4.8
|
33.3
|
1.0
|
|
CA
|
G:ASP478
|
4.9
|
32.5
|
1.0
|
|
CA
|
G:GLY452
|
4.9
|
27.0
|
1.0
|
|
C
|
G:ASP478
|
4.9
|
38.3
|
1.0
|
|
CA
|
G:SER479
|
5.0
|
34.9
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 4rjj
Go back to
Magnesium Binding Sites List in 4rjj
Magnesium binding site 8 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Acetolactate Synthase From Bacillus Subtilis Bound to Thdp - Crystal Form II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg602
b:36.6
occ:1.00
|
O
|
H:THR480
|
2.0
|
32.2
|
1.0
|
|
O
|
H:HOH762
|
2.0
|
32.2
|
1.0
|
|
O2A
|
H:TPP601
|
2.0
|
33.3
|
1.0
|
|
O3B
|
H:TPP601
|
2.2
|
27.7
|
1.0
|
|
OD1
|
H:ASP451
|
2.5
|
34.4
|
1.0
|
|
OD1
|
H:ASP478
|
2.7
|
36.1
|
1.0
|
|
PA
|
H:TPP601
|
3.1
|
36.3
|
1.0
|
|
C
|
H:THR480
|
3.2
|
41.2
|
1.0
|
|
PB
|
H:TPP601
|
3.4
|
25.3
|
1.0
|
|
O3A
|
H:TPP601
|
3.5
|
36.7
|
1.0
|
|
O7
|
H:TPP601
|
3.7
|
35.1
|
1.0
|
|
CG
|
H:ASP451
|
3.8
|
40.4
|
1.0
|
|
CG
|
H:ASP478
|
3.8
|
38.1
|
1.0
|
|
N
|
H:THR480
|
3.8
|
38.9
|
1.0
|
|
N
|
H:GLY452
|
3.9
|
30.2
|
1.0
|
|
CZ
|
H:PHE500
|
4.0
|
34.6
|
1.0
|
|
N
|
H:ASP451
|
4.1
|
24.9
|
1.0
|
|
CA
|
H:THR480
|
4.1
|
39.3
|
1.0
|
|
N
|
H:ASP482
|
4.2
|
34.8
|
1.0
|
|
N
|
H:TYR481
|
4.2
|
40.0
|
1.0
|
|
OD2
|
H:ASP478
|
4.3
|
38.4
|
1.0
|
|
CA
|
H:TYR481
|
4.3
|
37.1
|
1.0
|
|
O2B
|
H:TPP601
|
4.3
|
33.6
|
1.0
|
|
O1B
|
H:TPP601
|
4.4
|
21.8
|
1.0
|
|
OD2
|
H:ASP451
|
4.4
|
33.3
|
1.0
|
|
O1A
|
H:TPP601
|
4.4
|
29.0
|
1.0
|
|
CA
|
H:GLY452
|
4.5
|
29.0
|
1.0
|
|
OG1
|
H:THR480
|
4.7
|
37.4
|
1.0
|
|
N
|
H:SER479
|
4.7
|
40.5
|
1.0
|
|
CA
|
H:ASP451
|
4.7
|
25.4
|
1.0
|
|
CE2
|
H:PHE500
|
4.7
|
39.1
|
1.0
|
|
C
|
H:ASP451
|
4.7
|
27.0
|
1.0
|
|
C
|
H:GLY450
|
4.8
|
25.0
|
1.0
|
|
C
|
H:TYR481
|
4.8
|
37.5
|
1.0
|
|
CB
|
H:ASP482
|
4.8
|
34.4
|
1.0
|
|
CA
|
H:GLY450
|
4.9
|
24.1
|
1.0
|
|
CB
|
H:ASP451
|
4.9
|
31.3
|
1.0
|
|
C
|
H:SER479
|
4.9
|
40.2
|
1.0
|
|
CE1
|
H:PHE500
|
4.9
|
31.6
|
1.0
|
|
CB
|
H:ASP478
|
5.0
|
34.5
|
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 03:09:53 2024
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