Magnesium in PDB 4rjk: Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - Crystal Form II
Enzymatic activity of Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - Crystal Form II
All present enzymatic activity of Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - Crystal Form II:
4.1.3.18;
Protein crystallography data
The structure of Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - Crystal Form II, PDB code: 4rjk
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 /
2.50
|
|
Space group
|
P 21 2 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
111.510,
170.750,
342.590,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
16.6 /
21.7
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - Crystal Form II
(pdb code 4rjk). 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 Lthdp - Crystal Form II, PDB code: 4rjk:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 4rjk
Go back to
Magnesium Binding Sites List in 4rjk
Magnesium binding site 1 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - 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 Lthdp - Crystal Form II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg602
b:56.8
occ:1.00
|
O3B
|
A:TPP601
|
2.0
|
61.4
|
1.0
|
|
O
|
A:THR480
|
2.2
|
66.5
|
1.0
|
|
OD1
|
A:ASP451
|
2.3
|
71.7
|
1.0
|
|
O2A
|
A:TPP601
|
2.3
|
56.9
|
1.0
|
|
O
|
A:HOH791
|
2.5
|
63.2
|
1.0
|
|
OD1
|
A:ASP478
|
2.5
|
59.9
|
1.0
|
|
CG
|
A:ASP451
|
3.1
|
61.0
|
1.0
|
|
PB
|
A:TPP601
|
3.3
|
58.8
|
1.0
|
|
OD2
|
A:ASP451
|
3.4
|
66.5
|
1.0
|
|
C
|
A:THR480
|
3.4
|
68.3
|
1.0
|
|
PA
|
A:TPP601
|
3.4
|
64.7
|
1.0
|
|
O3A
|
A:TPP601
|
3.5
|
63.8
|
1.0
|
|
CG
|
A:ASP478
|
3.6
|
66.2
|
1.0
|
|
N
|
A:THR480
|
3.9
|
72.3
|
1.0
|
|
N
|
A:ASP451
|
4.1
|
57.4
|
1.0
|
|
O7
|
A:TPP601
|
4.1
|
57.8
|
1.0
|
|
OD2
|
A:ASP478
|
4.1
|
68.4
|
1.0
|
|
O1B
|
A:TPP601
|
4.2
|
49.9
|
1.0
|
|
N
|
A:ASP482
|
4.2
|
65.7
|
1.0
|
|
CA
|
A:THR480
|
4.3
|
70.2
|
1.0
|
|
N
|
A:GLY452
|
4.3
|
50.0
|
1.0
|
|
O2B
|
A:TPP601
|
4.3
|
57.8
|
1.0
|
|
N
|
A:TYR481
|
4.3
|
66.5
|
1.0
|
|
CZ
|
A:PHE500
|
4.4
|
63.1
|
1.0
|
|
CB
|
A:ASP451
|
4.5
|
56.7
|
1.0
|
|
CA
|
A:TYR481
|
4.5
|
62.0
|
1.0
|
|
N
|
A:SER479
|
4.6
|
72.3
|
1.0
|
|
CE2
|
A:TYR547
|
4.6
|
64.5
|
1.0
|
|
O1A
|
A:TPP601
|
4.6
|
60.1
|
1.0
|
|
CB
|
A:ASP478
|
4.7
|
58.7
|
1.0
|
|
CA
|
A:ASP451
|
4.7
|
57.7
|
1.0
|
|
O
|
A:TRP476
|
4.7
|
56.1
|
1.0
|
|
OG1
|
A:THR480
|
4.8
|
68.9
|
1.0
|
|
CB
|
A:ASP482
|
4.8
|
68.2
|
1.0
|
|
N
|
A:ASP478
|
4.8
|
60.9
|
1.0
|
|
CA
|
A:GLY450
|
4.8
|
48.5
|
1.0
|
|
C
|
A:GLY450
|
4.9
|
51.2
|
1.0
|
|
C
|
A:TYR481
|
4.9
|
68.8
|
1.0
|
|
C
|
A:SER479
|
5.0
|
69.7
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 4rjk
Go back to
Magnesium Binding Sites List in 4rjk
Magnesium binding site 2 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - 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 Lthdp - Crystal Form II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg602
b:57.3
occ:1.00
|
O3B
|
B:TPP601
|
2.1
|
50.9
|
1.0
|
|
O2A
|
B:TPP601
|
2.1
|
60.2
|
1.0
|
|
O
|
B:THR480
|
2.2
|
57.8
|
1.0
|
|
O
|
B:HOH812
|
2.2
|
56.5
|
1.0
|
|
OD1
|
B:ASP451
|
2.3
|
65.3
|
1.0
|
|
OD2
|
B:ASP478
|
3.1
|
63.9
|
1.0
|
|
C
|
B:THR480
|
3.3
|
58.5
|
1.0
|
|
CG
|
B:ASP451
|
3.4
|
65.5
|
1.0
|
|
PB
|
B:TPP601
|
3.5
|
56.5
|
1.0
|
|
PA
|
B:TPP601
|
3.5
|
60.5
|
1.0
|
|
N
|
B:THR480
|
3.7
|
63.9
|
1.0
|
|
CB
|
B:ASP478
|
3.7
|
66.0
|
1.0
|
|
OD2
|
B:ASP451
|
3.9
|
67.3
|
1.0
|
|
CG
|
B:ASP478
|
3.9
|
65.1
|
1.0
|
|
O3A
|
B:TPP601
|
3.9
|
55.2
|
1.0
|
|
N
|
B:ASP451
|
4.1
|
51.5
|
1.0
|
|
CA
|
B:THR480
|
4.1
|
61.8
|
1.0
|
|
N
|
B:GLY452
|
4.2
|
51.8
|
1.0
|
|
O2B
|
B:TPP601
|
4.3
|
53.9
|
1.0
|
|
N
|
B:SER479
|
4.4
|
73.6
|
1.0
|
|
O7
|
B:TPP601
|
4.4
|
58.5
|
1.0
|
|
N
|
B:TYR481
|
4.4
|
64.0
|
1.0
|
|
N
|
B:ASP482
|
4.4
|
62.5
|
1.0
|
|
O1B
|
B:TPP601
|
4.5
|
52.7
|
1.0
|
|
CZ
|
B:PHE500
|
4.5
|
58.5
|
1.0
|
|
O
|
B:TRP476
|
4.6
|
60.6
|
1.0
|
|
O1A
|
B:TPP601
|
4.6
|
57.9
|
1.0
|
|
CE2
|
B:TYR547
|
4.6
|
52.5
|
1.0
|
|
CA
|
B:ASP478
|
4.6
|
67.3
|
1.0
|
|
CB
|
B:ASP451
|
4.7
|
56.6
|
1.0
|
|
CA
|
B:TYR481
|
4.7
|
59.6
|
1.0
|
|
N
|
B:ASP478
|
4.7
|
65.2
|
1.0
|
|
C
|
B:ASP478
|
4.7
|
73.2
|
1.0
|
|
OG1
|
B:THR480
|
4.7
|
66.1
|
1.0
|
|
C
|
B:SER479
|
4.7
|
68.1
|
1.0
|
|
CA
|
B:ASP451
|
4.8
|
52.5
|
1.0
|
|
CA
|
B:GLY450
|
4.8
|
49.8
|
1.0
|
|
C
|
B:GLY450
|
4.9
|
51.3
|
1.0
|
|
C
|
B:ASP451
|
4.9
|
50.7
|
1.0
|
|
CB
|
B:ASP482
|
5.0
|
63.1
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 4rjk
Go back to
Magnesium Binding Sites List in 4rjk
Magnesium binding site 3 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - 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 Lthdp - Crystal Form II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg602
b:54.4
occ:1.00
|
O3B
|
C:TPP601
|
2.1
|
59.2
|
1.0
|
|
O2A
|
C:TPP601
|
2.2
|
53.3
|
1.0
|
|
O
|
C:HOH817
|
2.3
|
55.6
|
1.0
|
|
OD1
|
C:ASP451
|
2.4
|
56.5
|
1.0
|
|
O
|
C:THR480
|
2.4
|
57.8
|
1.0
|
|
OD2
|
C:ASP478
|
3.1
|
65.8
|
1.0
|
|
PB
|
C:TPP601
|
3.4
|
47.7
|
1.0
|
|
PA
|
C:TPP601
|
3.5
|
59.4
|
1.0
|
|
CB
|
C:ASP478
|
3.5
|
57.4
|
1.0
|
|
CG
|
C:ASP451
|
3.6
|
56.2
|
1.0
|
|
C
|
C:THR480
|
3.6
|
59.8
|
1.0
|
|
CG
|
C:ASP478
|
3.7
|
63.4
|
1.0
|
|
O3A
|
C:TPP601
|
3.7
|
57.6
|
1.0
|
|
N
|
C:ASP451
|
3.9
|
45.1
|
1.0
|
|
N
|
C:THR480
|
4.0
|
63.2
|
1.0
|
|
O2B
|
C:TPP601
|
4.1
|
55.6
|
1.0
|
|
N
|
C:GLY452
|
4.1
|
46.2
|
1.0
|
|
OD2
|
C:ASP451
|
4.1
|
58.2
|
1.0
|
|
N
|
C:SER479
|
4.3
|
67.8
|
1.0
|
|
O7
|
C:TPP601
|
4.3
|
50.1
|
1.0
|
|
O
|
C:TRP476
|
4.4
|
48.6
|
1.0
|
|
CA
|
C:THR480
|
4.4
|
59.7
|
1.0
|
|
N
|
C:ASP482
|
4.5
|
62.4
|
1.0
|
|
CA
|
C:ASP478
|
4.5
|
59.4
|
1.0
|
|
CZ
|
C:PHE500
|
4.5
|
53.9
|
1.0
|
|
N
|
C:ASP478
|
4.5
|
60.6
|
1.0
|
|
O1B
|
C:TPP601
|
4.5
|
47.8
|
1.0
|
|
CE2
|
C:TYR547
|
4.6
|
58.6
|
1.0
|
|
O1A
|
C:TPP601
|
4.6
|
51.2
|
1.0
|
|
N
|
C:TYR481
|
4.6
|
62.6
|
1.0
|
|
CA
|
C:ASP451
|
4.7
|
47.7
|
1.0
|
|
CB
|
C:ASP451
|
4.7
|
45.3
|
1.0
|
|
CA
|
C:GLY450
|
4.7
|
45.8
|
1.0
|
|
C
|
C:ASP478
|
4.8
|
70.3
|
1.0
|
|
C
|
C:GLY450
|
4.8
|
47.3
|
1.0
|
|
C
|
C:ASP451
|
4.8
|
46.6
|
1.0
|
|
CB
|
C:ASP482
|
4.8
|
55.9
|
1.0
|
|
CA
|
C:TYR481
|
4.8
|
60.2
|
1.0
|
|
OD1
|
C:ASP478
|
4.9
|
74.3
|
1.0
|
|
CA
|
C:GLY452
|
4.9
|
46.7
|
1.0
|
|
C
|
C:SER479
|
5.0
|
63.1
|
1.0
|
|
OG1
|
C:THR480
|
5.0
|
62.5
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 4rjk
Go back to
Magnesium Binding Sites List in 4rjk
Magnesium binding site 4 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - 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 Lthdp - Crystal Form II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg602
b:50.1
occ:1.00
|
O3B
|
D:TPP601
|
2.1
|
52.6
|
1.0
|
|
OD1
|
D:ASP451
|
2.2
|
53.7
|
1.0
|
|
O2A
|
D:TPP601
|
2.4
|
57.0
|
1.0
|
|
O
|
D:THR480
|
2.4
|
60.2
|
1.0
|
|
O
|
D:HOH707
|
2.5
|
50.8
|
1.0
|
|
CB
|
D:ASP478
|
3.2
|
57.6
|
1.0
|
|
OD2
|
D:ASP478
|
3.2
|
58.3
|
1.0
|
|
CG
|
D:ASP451
|
3.4
|
53.7
|
1.0
|
|
PB
|
D:TPP601
|
3.4
|
52.2
|
1.0
|
|
C
|
D:THR480
|
3.6
|
61.9
|
1.0
|
|
PA
|
D:TPP601
|
3.6
|
62.6
|
1.0
|
|
CG
|
D:ASP478
|
3.7
|
64.4
|
1.0
|
|
O3A
|
D:TPP601
|
3.8
|
58.4
|
1.0
|
|
OD2
|
D:ASP451
|
3.8
|
57.9
|
1.0
|
|
N
|
D:THR480
|
3.9
|
62.4
|
1.0
|
|
N
|
D:ASP451
|
3.9
|
43.6
|
1.0
|
|
N
|
D:SER479
|
4.1
|
61.8
|
1.0
|
|
O2B
|
D:TPP601
|
4.2
|
52.8
|
1.0
|
|
CA
|
D:ASP478
|
4.3
|
55.4
|
1.0
|
|
N
|
D:ASP478
|
4.3
|
53.4
|
1.0
|
|
CA
|
D:THR480
|
4.3
|
62.7
|
1.0
|
|
O
|
D:TRP476
|
4.4
|
48.4
|
1.0
|
|
N
|
D:GLY452
|
4.4
|
44.0
|
1.0
|
|
CE2
|
D:TYR547
|
4.4
|
50.8
|
1.0
|
|
O1B
|
D:TPP601
|
4.5
|
49.5
|
1.0
|
|
CZ
|
D:PHE500
|
4.5
|
48.8
|
1.0
|
|
O7
|
D:TPP601
|
4.5
|
51.8
|
1.0
|
|
N
|
D:ASP482
|
4.6
|
66.9
|
1.0
|
|
CB
|
D:ASP451
|
4.6
|
41.8
|
1.0
|
|
N
|
D:TYR481
|
4.7
|
65.0
|
1.0
|
|
CA
|
D:ASP451
|
4.7
|
43.8
|
1.0
|
|
C
|
D:ASP478
|
4.7
|
63.2
|
1.0
|
|
CA
|
D:GLY450
|
4.7
|
42.8
|
1.0
|
|
O1A
|
D:TPP601
|
4.7
|
60.3
|
1.0
|
|
C
|
D:GLY450
|
4.8
|
45.8
|
1.0
|
|
OG1
|
D:THR480
|
4.8
|
60.4
|
1.0
|
|
C
|
D:SER479
|
4.9
|
61.3
|
1.0
|
|
OD1
|
D:ASP478
|
4.9
|
79.6
|
1.0
|
|
CA
|
D:TYR481
|
4.9
|
62.6
|
1.0
|
|
CB
|
D:ASP482
|
4.9
|
58.8
|
1.0
|
|
CA
|
D:SER479
|
5.0
|
64.4
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 4rjk
Go back to
Magnesium Binding Sites List in 4rjk
Magnesium binding site 5 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - 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 Lthdp - Crystal Form II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg602
b:59.2
occ:1.00
|
O3B
|
E:TPP601
|
2.0
|
54.5
|
1.0
|
|
OD1
|
E:ASP478
|
2.1
|
68.0
|
1.0
|
|
O
|
E:THR480
|
2.1
|
64.7
|
1.0
|
|
O2A
|
E:TPP601
|
2.3
|
58.1
|
1.0
|
|
OD1
|
E:ASP451
|
2.5
|
58.8
|
1.0
|
|
O
|
E:HOH750
|
2.5
|
54.3
|
1.0
|
|
CG
|
E:ASP478
|
3.2
|
65.7
|
1.0
|
|
C
|
E:THR480
|
3.3
|
65.9
|
1.0
|
|
PB
|
E:TPP601
|
3.5
|
56.1
|
1.0
|
|
PA
|
E:TPP601
|
3.5
|
62.4
|
1.0
|
|
CG
|
E:ASP451
|
3.7
|
59.0
|
1.0
|
|
N
|
E:THR480
|
3.7
|
71.5
|
1.0
|
|
OD2
|
E:ASP478
|
3.7
|
65.5
|
1.0
|
|
O3A
|
E:TPP601
|
3.9
|
58.4
|
1.0
|
|
CA
|
E:THR480
|
4.1
|
70.9
|
1.0
|
|
N
|
E:GLY452
|
4.1
|
41.5
|
1.0
|
|
N
|
E:ASP451
|
4.1
|
52.3
|
1.0
|
|
CZ
|
E:PHE500
|
4.3
|
56.2
|
1.0
|
|
OD2
|
E:ASP451
|
4.3
|
60.7
|
1.0
|
|
O7
|
E:TPP601
|
4.3
|
56.5
|
1.0
|
|
N
|
E:TYR481
|
4.4
|
64.5
|
1.0
|
|
CB
|
E:ASP478
|
4.4
|
56.6
|
1.0
|
|
O1B
|
E:TPP601
|
4.4
|
46.9
|
1.0
|
|
O2B
|
E:TPP601
|
4.4
|
54.2
|
1.0
|
|
N
|
E:SER479
|
4.4
|
65.8
|
1.0
|
|
N
|
E:ASP482
|
4.5
|
59.9
|
1.0
|
|
CA
|
E:TYR481
|
4.7
|
62.3
|
1.0
|
|
OG1
|
E:THR480
|
4.7
|
72.6
|
1.0
|
|
O1A
|
E:TPP601
|
4.7
|
54.8
|
1.0
|
|
O
|
E:TRP476
|
4.7
|
46.0
|
1.0
|
|
N
|
E:ASP478
|
4.7
|
55.2
|
1.0
|
|
C
|
E:SER479
|
4.7
|
66.5
|
1.0
|
|
CE2
|
E:TYR547
|
4.7
|
58.8
|
1.0
|
|
CB
|
E:ASP482
|
4.9
|
63.7
|
1.0
|
|
CA
|
E:ASP451
|
4.9
|
48.8
|
1.0
|
|
CB
|
E:ASP451
|
4.9
|
42.8
|
1.0
|
|
CA
|
E:GLY450
|
4.9
|
41.6
|
1.0
|
|
CA
|
E:GLY452
|
4.9
|
50.8
|
1.0
|
|
C
|
E:ASP478
|
4.9
|
64.1
|
1.0
|
|
CA
|
E:ASP478
|
4.9
|
60.6
|
1.0
|
|
C
|
E:GLY450
|
4.9
|
46.9
|
1.0
|
|
C
|
E:ASP451
|
5.0
|
47.4
|
1.0
|
|
CA
|
E:SER479
|
5.0
|
66.2
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 4rjk
Go back to
Magnesium Binding Sites List in 4rjk
Magnesium binding site 6 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - 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 Lthdp - Crystal Form II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg602
b:53.4
occ:1.00
|
O3B
|
F:TPP601
|
2.1
|
51.5
|
1.0
|
|
OD1
|
F:ASP478
|
2.1
|
61.9
|
1.0
|
|
O2A
|
F:TPP601
|
2.2
|
52.9
|
1.0
|
|
OD1
|
F:ASP451
|
2.2
|
59.0
|
1.0
|
|
O
|
F:THR480
|
2.3
|
58.1
|
1.0
|
|
O
|
F:HOH819
|
2.4
|
55.9
|
1.0
|
|
CG
|
F:ASP478
|
3.2
|
63.8
|
1.0
|
|
CG
|
F:ASP451
|
3.4
|
59.5
|
1.0
|
|
C
|
F:THR480
|
3.5
|
65.9
|
1.0
|
|
PB
|
F:TPP601
|
3.5
|
51.9
|
1.0
|
|
PA
|
F:TPP601
|
3.5
|
60.3
|
1.0
|
|
OD2
|
F:ASP478
|
3.8
|
59.6
|
1.0
|
|
N
|
F:THR480
|
3.8
|
62.5
|
1.0
|
|
O3A
|
F:TPP601
|
3.9
|
58.6
|
1.0
|
|
OD2
|
F:ASP451
|
3.9
|
61.6
|
1.0
|
|
N
|
F:ASP451
|
4.0
|
46.3
|
1.0
|
|
N
|
F:GLY452
|
4.1
|
48.1
|
1.0
|
|
O2B
|
F:TPP601
|
4.2
|
59.3
|
1.0
|
|
CA
|
F:THR480
|
4.2
|
64.0
|
1.0
|
|
O7
|
F:TPP601
|
4.3
|
54.6
|
1.0
|
|
N
|
F:SER479
|
4.4
|
64.5
|
1.0
|
|
CZ
|
F:PHE500
|
4.4
|
59.4
|
1.0
|
|
CB
|
F:ASP478
|
4.4
|
50.3
|
1.0
|
|
N
|
F:TYR481
|
4.5
|
65.0
|
1.0
|
|
N
|
F:ASP478
|
4.5
|
58.8
|
1.0
|
|
O1B
|
F:TPP601
|
4.5
|
49.1
|
1.0
|
|
N
|
F:ASP482
|
4.5
|
56.2
|
1.0
|
|
O
|
F:TRP476
|
4.6
|
51.7
|
1.0
|
|
O1A
|
F:TPP601
|
4.6
|
58.1
|
1.0
|
|
CB
|
F:ASP451
|
4.6
|
44.4
|
1.0
|
|
CA
|
F:ASP451
|
4.7
|
46.7
|
1.0
|
|
CE2
|
F:TYR547
|
4.7
|
53.6
|
1.0
|
|
C
|
F:SER479
|
4.8
|
63.9
|
1.0
|
|
CA
|
F:GLY450
|
4.8
|
49.0
|
1.0
|
|
C
|
F:ASP478
|
4.8
|
69.0
|
1.0
|
|
C
|
F:GLY450
|
4.8
|
44.1
|
1.0
|
|
CA
|
F:TYR481
|
4.8
|
62.5
|
1.0
|
|
C
|
F:ASP451
|
4.8
|
51.0
|
1.0
|
|
CA
|
F:ASP478
|
4.8
|
61.4
|
1.0
|
|
CA
|
F:GLY452
|
4.8
|
53.5
|
1.0
|
|
OG1
|
F:THR480
|
4.9
|
58.6
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 4rjk
Go back to
Magnesium Binding Sites List in 4rjk
Magnesium binding site 7 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - 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 Lthdp - Crystal Form II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg602
b:49.1
occ:1.00
|
O2A
|
G:TPP601
|
2.0
|
52.9
|
1.0
|
|
O3B
|
G:TPP601
|
2.1
|
49.2
|
1.0
|
|
OD1
|
G:ASP478
|
2.2
|
60.5
|
1.0
|
|
O
|
G:THR480
|
2.2
|
59.4
|
1.0
|
|
O
|
G:HOH738
|
2.3
|
54.2
|
1.0
|
|
OD1
|
G:ASP451
|
2.3
|
57.5
|
1.0
|
|
CG
|
G:ASP478
|
3.3
|
62.4
|
1.0
|
|
PA
|
G:TPP601
|
3.4
|
63.4
|
1.0
|
|
C
|
G:THR480
|
3.4
|
63.2
|
1.0
|
|
PB
|
G:TPP601
|
3.5
|
52.6
|
1.0
|
|
CG
|
G:ASP451
|
3.5
|
58.1
|
1.0
|
|
O3A
|
G:TPP601
|
3.8
|
55.3
|
1.0
|
|
OD2
|
G:ASP478
|
3.8
|
56.2
|
1.0
|
|
N
|
G:THR480
|
3.9
|
61.3
|
1.0
|
|
N
|
G:ASP451
|
4.0
|
52.5
|
1.0
|
|
OD2
|
G:ASP451
|
4.1
|
60.8
|
1.0
|
|
N
|
G:GLY452
|
4.2
|
52.5
|
1.0
|
|
O7
|
G:TPP601
|
4.2
|
56.8
|
1.0
|
|
CA
|
G:THR480
|
4.2
|
60.8
|
1.0
|
|
CZ
|
G:PHE500
|
4.3
|
57.4
|
1.0
|
|
O2B
|
G:TPP601
|
4.3
|
56.2
|
1.0
|
|
N
|
G:TYR481
|
4.4
|
62.5
|
1.0
|
|
N
|
G:ASP482
|
4.4
|
57.5
|
1.0
|
|
CB
|
G:ASP478
|
4.4
|
57.1
|
1.0
|
|
O1A
|
G:TPP601
|
4.4
|
60.5
|
1.0
|
|
O1B
|
G:TPP601
|
4.5
|
50.0
|
1.0
|
|
N
|
G:SER479
|
4.5
|
65.4
|
1.0
|
|
O
|
G:TRP476
|
4.5
|
51.2
|
1.0
|
|
CA
|
G:TYR481
|
4.6
|
56.7
|
1.0
|
|
N
|
G:ASP478
|
4.6
|
57.7
|
1.0
|
|
CB
|
G:ASP451
|
4.7
|
45.5
|
1.0
|
|
CA
|
G:GLY450
|
4.7
|
45.8
|
1.0
|
|
CA
|
G:ASP451
|
4.7
|
49.5
|
1.0
|
|
OG1
|
G:THR480
|
4.8
|
57.3
|
1.0
|
|
C
|
G:GLY450
|
4.8
|
49.8
|
1.0
|
|
CE2
|
G:TYR547
|
4.9
|
55.1
|
1.0
|
|
CA
|
G:ASP478
|
4.9
|
55.8
|
1.0
|
|
C
|
G:ASP478
|
4.9
|
62.5
|
1.0
|
|
C
|
G:ASP451
|
4.9
|
50.8
|
1.0
|
|
C
|
G:SER479
|
4.9
|
63.6
|
1.0
|
|
CB
|
G:ASP482
|
5.0
|
57.7
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 4rjk
Go back to
Magnesium Binding Sites List in 4rjk
Magnesium binding site 8 out
of 8 in the Acetolactate Synthase From Bacillus Subtilis Bound to Lthdp - 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 Lthdp - Crystal Form II within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg602
b:55.0
occ:1.00
|
O1B
|
H:TDL601
|
2.0
|
57.9
|
1.0
|
|
O
|
H:THR480
|
2.2
|
68.2
|
1.0
|
|
O2A
|
H:TDL601
|
2.2
|
60.0
|
1.0
|
|
O
|
H:HOH760
|
2.3
|
61.5
|
1.0
|
|
OD1
|
H:ASP478
|
2.4
|
62.8
|
1.0
|
|
OD1
|
H:ASP451
|
2.4
|
61.7
|
1.0
|
|
PB
|
H:TDL601
|
3.2
|
53.7
|
1.0
|
|
C
|
H:THR480
|
3.3
|
66.0
|
1.0
|
|
PA
|
H:TDL601
|
3.4
|
67.7
|
1.0
|
|
O3A
|
H:TDL601
|
3.4
|
59.8
|
1.0
|
|
CG
|
H:ASP478
|
3.5
|
63.6
|
1.0
|
|
CG
|
H:ASP451
|
3.6
|
63.6
|
1.0
|
|
N
|
H:THR480
|
3.8
|
66.1
|
1.0
|
|
OD2
|
H:ASP478
|
3.9
|
64.5
|
1.0
|
|
O2B
|
H:TDL601
|
4.0
|
63.8
|
1.0
|
|
N
|
H:ASP451
|
4.0
|
54.8
|
1.0
|
|
CA
|
H:THR480
|
4.1
|
66.8
|
1.0
|
|
O7
|
H:TDL601
|
4.1
|
60.4
|
1.0
|
|
N
|
H:GLY452
|
4.1
|
48.4
|
1.0
|
|
OD2
|
H:ASP451
|
4.2
|
58.5
|
1.0
|
|
O3B
|
H:TDL601
|
4.4
|
44.5
|
1.0
|
|
N
|
H:TYR481
|
4.4
|
67.4
|
1.0
|
|
O
|
H:TRP476
|
4.5
|
48.6
|
1.0
|
|
N
|
H:ASP482
|
4.5
|
59.9
|
1.0
|
|
CZ
|
H:PHE500
|
4.5
|
61.1
|
1.0
|
|
O1A
|
H:TDL601
|
4.5
|
61.0
|
1.0
|
|
CE2
|
H:TYR547
|
4.6
|
57.9
|
1.0
|
|
CA
|
H:GLY450
|
4.7
|
45.0
|
1.0
|
|
CB
|
H:ASP478
|
4.7
|
49.6
|
1.0
|
|
N
|
H:ASP478
|
4.7
|
58.0
|
1.0
|
|
CA
|
H:TYR481
|
4.7
|
63.8
|
1.0
|
|
N
|
H:SER479
|
4.7
|
68.3
|
1.0
|
|
C
|
H:GLY450
|
4.8
|
47.8
|
1.0
|
|
CA
|
H:ASP451
|
4.8
|
54.0
|
1.0
|
|
CB
|
H:ASP451
|
4.8
|
57.4
|
1.0
|
|
CB
|
H:THR480
|
4.8
|
66.1
|
1.0
|
|
CA
|
H:GLY452
|
4.9
|
53.7
|
1.0
|
|
CB
|
H:ASP482
|
4.9
|
65.2
|
1.0
|
|
C
|
H:SER479
|
5.0
|
63.9
|
1.0
|
|
C
|
H:ASP451
|
5.0
|
49.2
|
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.
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