Magnesium in PDB 5wdg: Acetolactate Synthase From Klebsiella Pneumoniae in Complex with A Reaction Intermediate
Enzymatic activity of Acetolactate Synthase From Klebsiella Pneumoniae in Complex with A Reaction Intermediate
All present enzymatic activity of Acetolactate Synthase From Klebsiella Pneumoniae in Complex with A Reaction Intermediate:
2.2.1.6;
Protein crystallography data
The structure of Acetolactate Synthase From Klebsiella Pneumoniae in Complex with A Reaction Intermediate, PDB code: 5wdg
was solved by
A.J.Latta,
F.H.Andrews,
M.J.Mcleish,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
55.12 /
2.12
|
|
Space group
|
I 1 2 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
85.470,
134.410,
110.745,
90.00,
95.45,
90.00
|
|
R / Rfree (%)
|
20.4 /
24.7
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with A Reaction Intermediate
(pdb code 5wdg). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the
Acetolactate Synthase From Klebsiella Pneumoniae in Complex with A Reaction Intermediate, PDB code: 5wdg:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
Magnesium binding site 1 out
of 6 in 5wdg
Go back to
Magnesium Binding Sites List in 5wdg
Magnesium binding site 1 out
of 6 in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with A Reaction Intermediate
 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 Klebsiella Pneumoniae in Complex with A Reaction Intermediate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg601
b:44.3
occ:1.00
|
O
|
A:HOH729
|
1.9
|
41.7
|
1.0
|
|
O07
|
A:A4Y605
|
2.0
|
43.1
|
1.0
|
|
OD1
|
A:ASP447
|
2.0
|
48.0
|
1.0
|
|
OD1
|
A:ASP474
|
2.1
|
62.1
|
1.0
|
|
O08
|
A:A4Y605
|
2.2
|
40.5
|
1.0
|
|
O
|
A:GLY476
|
2.3
|
52.6
|
1.0
|
|
CG
|
A:ASP447
|
2.9
|
48.1
|
1.0
|
|
H
|
A:GLY476
|
3.1
|
70.4
|
1.0
|
|
H
|
A:ASP447
|
3.2
|
57.1
|
1.0
|
|
P04
|
A:A4Y605
|
3.2
|
54.8
|
1.0
|
|
OD2
|
A:ASP447
|
3.2
|
48.9
|
1.0
|
|
CG
|
A:ASP474
|
3.2
|
61.9
|
1.0
|
|
H
|
A:GLY448
|
3.3
|
58.3
|
1.0
|
|
P02
|
A:A4Y605
|
3.4
|
43.8
|
1.0
|
|
C
|
A:GLY476
|
3.5
|
53.8
|
1.0
|
|
H
|
A:ASP474
|
3.5
|
69.9
|
1.0
|
|
HZ
|
A:PHE496
|
3.6
|
71.1
|
1.0
|
|
O05
|
A:A4Y605
|
3.6
|
78.9
|
1.0
|
|
O03
|
A:A4Y605
|
3.6
|
42.9
|
1.0
|
|
H
|
A:ASN478
|
3.7
|
59.5
|
1.0
|
|
OD2
|
A:ASP474
|
3.9
|
62.7
|
1.0
|
|
N
|
A:ASP447
|
3.9
|
47.6
|
1.0
|
|
N
|
A:GLY476
|
3.9
|
58.7
|
1.0
|
|
HA
|
A:TYR477
|
4.0
|
60.0
|
1.0
|
|
HA3
|
A:GLY446
|
4.0
|
55.6
|
1.0
|
|
N
|
A:GLY448
|
4.1
|
48.6
|
1.0
|
|
O09
|
A:A4Y605
|
4.1
|
39.0
|
1.0
|
|
H
|
A:ASN475
|
4.1
|
73.9
|
1.0
|
|
CB
|
A:ASP447
|
4.2
|
47.6
|
1.0
|
|
O
|
A:TRP472
|
4.3
|
57.5
|
1.0
|
|
N
|
A:ASP474
|
4.3
|
58.2
|
1.0
|
|
CA
|
A:GLY476
|
4.3
|
56.5
|
1.0
|
|
HE2
|
A:TYR543
|
4.3
|
75.0
|
1.0
|
|
CB
|
A:ASP474
|
4.4
|
60.5
|
1.0
|
|
CZ
|
A:PHE496
|
4.4
|
59.2
|
1.0
|
|
O06
|
A:A4Y605
|
4.4
|
20.6
|
1.0
|
|
N
|
A:ASN475
|
4.5
|
61.6
|
1.0
|
|
N
|
A:TYR477
|
4.5
|
52.8
|
1.0
|
|
N
|
A:ASN478
|
4.5
|
49.6
|
1.0
|
|
HB3
|
A:ASP474
|
4.5
|
72.6
|
1.0
|
|
HB2
|
A:ASN478
|
4.5
|
60.2
|
1.0
|
|
CA
|
A:ASP447
|
4.5
|
47.4
|
1.0
|
|
O01
|
A:A4Y605
|
4.5
|
33.9
|
1.0
|
|
CA
|
A:TYR477
|
4.6
|
50.0
|
1.0
|
|
CA
|
A:GLY446
|
4.7
|
46.4
|
1.0
|
|
CA
|
A:ASP474
|
4.7
|
59.7
|
1.0
|
|
HA2
|
A:GLY446
|
4.7
|
55.6
|
1.0
|
|
C
|
A:GLY446
|
4.7
|
46.7
|
1.0
|
|
HA
|
A:VAL473
|
4.7
|
69.0
|
1.0
|
|
HA3
|
A:GLY448
|
4.7
|
57.0
|
1.0
|
|
HB3
|
A:ASP447
|
4.8
|
57.2
|
1.0
|
|
C
|
A:ASP474
|
4.8
|
60.4
|
1.0
|
|
C
|
A:ASP447
|
4.8
|
48.5
|
1.0
|
|
HD2
|
A:TYR477
|
4.8
|
54.5
|
1.0
|
|
HB2
|
A:ASP447
|
4.8
|
57.2
|
1.0
|
|
HA3
|
A:GLY476
|
4.8
|
67.8
|
1.0
|
|
HE2
|
A:PHE496
|
4.8
|
70.7
|
1.0
|
|
HB3
|
A:ASN478
|
4.8
|
60.2
|
1.0
|
|
HH
|
A:TYR543
|
5.0
|
74.0
|
1.0
|
|
C
|
A:ASN475
|
5.0
|
60.7
|
1.0
|
|
Magnesium binding site 2 out
of 6 in 5wdg
Go back to
Magnesium Binding Sites List in 5wdg
Magnesium binding site 2 out
of 6 in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with A Reaction Intermediate
 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 Klebsiella Pneumoniae in Complex with A Reaction Intermediate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg602
b:50.0
occ:1.00
|
O
|
A:HOH868
|
2.3
|
45.5
|
1.0
|
|
O
|
A:ARG69
|
2.4
|
38.8
|
1.0
|
|
OE1
|
A:GLN220
|
2.6
|
34.8
|
1.0
|
|
O
|
A:HOH842
|
2.7
|
49.4
|
1.0
|
|
O
|
A:HOH810
|
3.0
|
31.1
|
1.0
|
|
O
|
A:HOH848
|
3.2
|
48.5
|
1.0
|
|
HD3
|
A:PRO221
|
3.2
|
42.9
|
1.0
|
|
HA
|
A:GLN220
|
3.4
|
41.0
|
1.0
|
|
HD2
|
A:PRO221
|
3.6
|
42.9
|
1.0
|
|
C
|
A:ARG69
|
3.6
|
39.4
|
1.0
|
|
CD
|
A:GLN220
|
3.6
|
34.1
|
1.0
|
|
HA
|
A:ARG69
|
3.7
|
46.6
|
1.0
|
|
HE22
|
A:GLN220
|
3.8
|
41.3
|
1.0
|
|
CD
|
A:PRO221
|
3.8
|
35.8
|
1.0
|
|
HG2
|
A:ARG69
|
3.8
|
44.6
|
1.0
|
|
HG3
|
A:ARG69
|
3.9
|
44.6
|
1.0
|
|
O
|
A:HOH793
|
4.0
|
24.3
|
1.0
|
|
NE2
|
A:GLN220
|
4.1
|
34.4
|
1.0
|
|
CA
|
A:ARG69
|
4.2
|
38.8
|
1.0
|
|
CG
|
A:ARG69
|
4.3
|
37.2
|
1.0
|
|
O
|
A:HOH845
|
4.3
|
37.6
|
1.0
|
|
CA
|
A:GLN220
|
4.4
|
34.1
|
1.0
|
|
HA
|
A:ILE70
|
4.5
|
47.4
|
1.0
|
|
HA2
|
A:GLY72
|
4.6
|
45.5
|
1.0
|
|
HB3
|
A:GLN220
|
4.6
|
40.7
|
1.0
|
|
HG3
|
A:PRO221
|
4.6
|
43.8
|
1.0
|
|
O
|
A:HOH775
|
4.6
|
40.5
|
1.0
|
|
N
|
A:ILE70
|
4.7
|
39.9
|
1.0
|
|
O
|
A:SER219
|
4.7
|
35.0
|
1.0
|
|
H
|
A:GLY72
|
4.7
|
45.1
|
1.0
|
|
O
|
A:ILE70
|
4.8
|
38.0
|
1.0
|
|
CG
|
A:GLN220
|
4.8
|
34.4
|
1.0
|
|
CB
|
A:GLN220
|
4.8
|
33.9
|
1.0
|
|
CG
|
A:PRO221
|
4.8
|
36.5
|
1.0
|
|
O
|
A:GLY68
|
4.8
|
36.1
|
1.0
|
|
CB
|
A:ARG69
|
4.9
|
37.6
|
1.0
|
|
N
|
A:PRO221
|
4.9
|
35.7
|
1.0
|
|
HE21
|
A:GLN220
|
4.9
|
41.3
|
1.0
|
|
CA
|
A:ILE70
|
4.9
|
39.5
|
1.0
|
|
C
|
A:ILE70
|
4.9
|
39.0
|
1.0
|
|
Magnesium binding site 3 out
of 6 in 5wdg
Go back to
Magnesium Binding Sites List in 5wdg
Magnesium binding site 3 out
of 6 in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with A Reaction Intermediate
 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 Klebsiella Pneumoniae in Complex with A Reaction Intermediate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg603
b:43.1
occ:1.00
|
O
|
A:HOH890
|
2.2
|
53.0
|
1.0
|
|
O
|
A:HOH804
|
2.3
|
53.8
|
1.0
|
|
O
|
A:HOH833
|
2.4
|
29.2
|
1.0
|
|
O
|
A:THR132
|
2.5
|
27.8
|
1.0
|
|
O
|
A:SER129
|
2.6
|
28.3
|
1.0
|
|
O
|
A:HOH882
|
2.7
|
36.0
|
1.0
|
|
C
|
A:SER129
|
3.7
|
28.3
|
1.0
|
|
C
|
A:THR132
|
3.7
|
27.6
|
1.0
|
|
HA
|
A:SER129
|
3.7
|
33.2
|
1.0
|
|
H
|
A:THR132
|
3.8
|
31.9
|
1.0
|
|
O
|
A:HOH902
|
4.0
|
43.5
|
1.0
|
|
HA
|
A:LYS133
|
4.1
|
33.3
|
1.0
|
|
HB3
|
A:SER129
|
4.1
|
35.0
|
1.0
|
|
CA
|
A:SER129
|
4.2
|
27.7
|
1.0
|
|
HG1
|
A:THR132
|
4.3
|
32.7
|
1.0
|
|
C
|
A:LYS133
|
4.4
|
28.1
|
1.0
|
|
OG1
|
A:THR132
|
4.4
|
27.2
|
1.0
|
|
O
|
A:LYS133
|
4.4
|
28.9
|
1.0
|
|
HA
|
A:PRO130
|
4.5
|
33.7
|
1.0
|
|
N
|
A:THR132
|
4.5
|
26.6
|
1.0
|
|
CA
|
A:LYS133
|
4.5
|
27.8
|
1.0
|
|
N
|
A:LYS133
|
4.6
|
28.3
|
1.0
|
|
CB
|
A:SER129
|
4.7
|
29.2
|
1.0
|
|
CA
|
A:THR132
|
4.7
|
26.9
|
1.0
|
|
N
|
A:PRO130
|
4.7
|
27.8
|
1.0
|
|
N
|
A:TYR134
|
4.7
|
27.2
|
1.0
|
|
H
|
A:TYR134
|
4.9
|
32.6
|
1.0
|
|
CA
|
A:PRO130
|
4.9
|
28.1
|
1.0
|
|
Magnesium binding site 4 out
of 6 in 5wdg
Go back to
Magnesium Binding Sites List in 5wdg
Magnesium binding site 4 out
of 6 in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with A Reaction Intermediate
 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 Klebsiella Pneumoniae in Complex with A Reaction Intermediate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg601
b:27.6
occ:1.00
|
OD1
|
B:ASP474
|
2.0
|
39.4
|
1.0
|
|
O
|
B:HOH765
|
2.0
|
32.8
|
1.0
|
|
O06
|
B:A4Y605
|
2.1
|
28.0
|
1.0
|
|
O
|
B:GLY476
|
2.1
|
28.0
|
1.0
|
|
OD1
|
B:ASP447
|
2.2
|
34.1
|
1.0
|
|
O08
|
B:A4Y605
|
2.3
|
19.2
|
1.0
|
|
H
|
B:GLY476
|
3.1
|
39.8
|
1.0
|
|
CG
|
B:ASP474
|
3.1
|
39.7
|
1.0
|
|
CG
|
B:ASP447
|
3.2
|
32.3
|
1.0
|
|
P04
|
B:A4Y605
|
3.2
|
28.8
|
1.0
|
|
H
|
B:ASP447
|
3.3
|
36.6
|
1.0
|
|
C
|
B:GLY476
|
3.3
|
28.6
|
1.0
|
|
H
|
B:GLY448
|
3.4
|
36.6
|
1.0
|
|
H
|
B:ASN478
|
3.5
|
32.5
|
1.0
|
|
P02
|
B:A4Y605
|
3.5
|
27.8
|
1.0
|
|
OD2
|
B:ASP447
|
3.5
|
32.7
|
1.0
|
|
O03
|
B:A4Y605
|
3.6
|
26.9
|
1.0
|
|
OD2
|
B:ASP474
|
3.6
|
40.2
|
1.0
|
|
H
|
B:ASP474
|
3.7
|
46.9
|
1.0
|
|
HZ
|
B:PHE496
|
3.7
|
37.1
|
1.0
|
|
O07
|
B:A4Y605
|
3.7
|
36.2
|
1.0
|
|
HA
|
B:TYR477
|
3.8
|
32.7
|
1.0
|
|
N
|
B:GLY476
|
3.9
|
33.1
|
1.0
|
|
N
|
B:ASP447
|
4.0
|
30.5
|
1.0
|
|
HA3
|
B:GLY446
|
4.1
|
38.1
|
1.0
|
|
N
|
B:GLY448
|
4.2
|
30.5
|
1.0
|
|
HE1
|
B:TYR543
|
4.2
|
44.3
|
1.0
|
|
CA
|
B:GLY476
|
4.2
|
30.3
|
1.0
|
|
N
|
B:ASN478
|
4.3
|
27.1
|
1.0
|
|
H
|
B:ASN475
|
4.3
|
47.4
|
1.0
|
|
N
|
B:TYR477
|
4.3
|
27.6
|
1.0
|
|
CB
|
B:ASP474
|
4.3
|
39.6
|
1.0
|
|
N
|
B:ASP474
|
4.4
|
39.1
|
1.0
|
|
HB2
|
B:ASN478
|
4.4
|
32.4
|
1.0
|
|
O
|
B:TRP472
|
4.4
|
36.5
|
1.0
|
|
O09
|
B:A4Y605
|
4.4
|
28.3
|
1.0
|
|
HB3
|
B:ASP474
|
4.5
|
47.5
|
1.0
|
|
CB
|
B:ASP447
|
4.5
|
31.1
|
1.0
|
|
CA
|
B:TYR477
|
4.5
|
27.2
|
1.0
|
|
O05
|
B:A4Y605
|
4.5
|
15.7
|
1.0
|
|
CZ
|
B:PHE496
|
4.5
|
30.9
|
1.0
|
|
O01
|
B:A4Y605
|
4.5
|
30.8
|
1.0
|
|
N
|
B:ASN475
|
4.6
|
39.5
|
1.0
|
|
CA
|
B:ASP447
|
4.6
|
31.0
|
1.0
|
|
HB3
|
B:ASN478
|
4.7
|
32.4
|
1.0
|
|
HA3
|
B:GLY476
|
4.7
|
36.3
|
1.0
|
|
CA
|
B:ASP474
|
4.7
|
39.6
|
1.0
|
|
CA
|
B:GLY446
|
4.7
|
31.7
|
1.0
|
|
HA3
|
B:GLY448
|
4.7
|
34.1
|
1.0
|
|
HA2
|
B:GLY446
|
4.8
|
38.1
|
1.0
|
|
C
|
B:GLY446
|
4.8
|
31.2
|
1.0
|
|
HD2
|
B:TYR477
|
4.8
|
31.0
|
1.0
|
|
C
|
B:ASP474
|
4.8
|
40.2
|
1.0
|
|
CB
|
B:ASN478
|
4.9
|
27.0
|
1.0
|
|
C
|
B:ASP447
|
4.9
|
31.6
|
1.0
|
|
HH
|
B:TYR543
|
4.9
|
44.8
|
1.0
|
|
HE2
|
B:PHE496
|
4.9
|
37.0
|
1.0
|
|
C
|
B:TYR477
|
4.9
|
26.9
|
1.0
|
|
HA
|
B:VAL473
|
4.9
|
45.9
|
1.0
|
|
HA2
|
B:GLY476
|
4.9
|
36.3
|
1.0
|
|
HB3
|
B:ASP447
|
5.0
|
37.3
|
1.0
|
|
Magnesium binding site 5 out
of 6 in 5wdg
Go back to
Magnesium Binding Sites List in 5wdg
Magnesium binding site 5 out
of 6 in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with A Reaction Intermediate
 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 Klebsiella Pneumoniae in Complex with A Reaction Intermediate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg602
b:46.1
occ:1.00
|
O
|
B:SER129
|
2.3
|
26.1
|
1.0
|
|
O
|
B:THR132
|
2.4
|
24.5
|
1.0
|
|
O
|
B:HOH834
|
2.5
|
25.3
|
1.0
|
|
O
|
B:HOH899
|
2.9
|
43.0
|
1.0
|
|
O
|
B:HOH950
|
3.0
|
37.2
|
1.0
|
|
C
|
B:SER129
|
3.4
|
25.4
|
1.0
|
|
H
|
B:THR132
|
3.6
|
29.6
|
1.0
|
|
C
|
B:THR132
|
3.6
|
24.7
|
1.0
|
|
HA
|
B:SER129
|
3.6
|
30.6
|
1.0
|
|
CA
|
B:SER129
|
4.0
|
25.5
|
1.0
|
|
HG1
|
B:THR132
|
4.0
|
28.1
|
1.0
|
|
HA
|
B:LYS133
|
4.0
|
29.5
|
1.0
|
|
HB3
|
B:SER129
|
4.0
|
34.1
|
1.0
|
|
OG1
|
B:THR132
|
4.2
|
23.4
|
1.0
|
|
HA
|
B:PRO130
|
4.3
|
29.8
|
1.0
|
|
N
|
B:THR132
|
4.3
|
24.6
|
1.0
|
|
C
|
B:LYS133
|
4.3
|
24.0
|
1.0
|
|
O
|
B:LYS133
|
4.4
|
23.2
|
1.0
|
|
CA
|
B:LYS133
|
4.5
|
24.6
|
1.0
|
|
CA
|
B:THR132
|
4.5
|
25.0
|
1.0
|
|
N
|
B:LYS133
|
4.5
|
24.2
|
1.0
|
|
N
|
B:PRO130
|
4.5
|
23.4
|
1.0
|
|
CB
|
B:SER129
|
4.6
|
28.4
|
1.0
|
|
N
|
B:TYR134
|
4.7
|
23.4
|
1.0
|
|
CA
|
B:PRO130
|
4.7
|
24.8
|
1.0
|
|
H
|
B:TYR134
|
4.8
|
28.1
|
1.0
|
|
O
|
B:HOH821
|
4.8
|
48.3
|
1.0
|
|
C
|
B:PRO130
|
4.8
|
25.7
|
1.0
|
|
H
|
B:VAL131
|
4.9
|
31.1
|
1.0
|
|
N
|
B:VAL131
|
5.0
|
25.9
|
1.0
|
|
CB
|
B:THR132
|
5.0
|
25.4
|
1.0
|
|
Magnesium binding site 6 out
of 6 in 5wdg
Go back to
Magnesium Binding Sites List in 5wdg
Magnesium binding site 6 out
of 6 in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with A Reaction Intermediate
 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 Klebsiella Pneumoniae in Complex with A Reaction Intermediate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg603
b:54.8
occ:1.00
|
O
|
B:LEU44
|
2.4
|
28.2
|
1.0
|
|
O
|
B:ILE49
|
2.4
|
31.8
|
1.0
|
|
O
|
B:HOH923
|
2.6
|
36.3
|
1.0
|
|
O
|
B:SER47
|
2.7
|
36.6
|
1.0
|
|
O
|
B:HOH896
|
3.1
|
33.8
|
1.0
|
|
HA
|
B:LEU45
|
3.3
|
43.1
|
1.0
|
|
H
|
B:SER47
|
3.5
|
41.3
|
1.0
|
|
C
|
B:LEU44
|
3.5
|
31.5
|
1.0
|
|
C
|
B:ILE49
|
3.6
|
31.5
|
1.0
|
|
C
|
B:SER47
|
3.7
|
36.0
|
1.0
|
|
HA
|
B:ARG50
|
3.8
|
37.6
|
1.0
|
|
O
|
B:LEU45
|
3.8
|
37.3
|
1.0
|
|
HG13
|
B:ILE51
|
3.9
|
33.7
|
1.0
|
|
CA
|
B:LEU45
|
3.9
|
35.9
|
1.0
|
|
HB3
|
B:SER47
|
3.9
|
44.6
|
1.0
|
|
HB3
|
B:LEU44
|
4.0
|
37.0
|
1.0
|
|
C
|
B:LEU45
|
4.0
|
36.3
|
1.0
|
|
N
|
B:LEU45
|
4.2
|
34.2
|
1.0
|
|
N
|
B:SER47
|
4.2
|
34.4
|
1.0
|
|
N
|
B:ILE49
|
4.2
|
33.5
|
1.0
|
|
H
|
B:ILE49
|
4.3
|
40.2
|
1.0
|
|
H
|
B:ILE51
|
4.3
|
35.0
|
1.0
|
|
CA
|
B:SER47
|
4.4
|
35.7
|
1.0
|
|
C
|
B:SER48
|
4.4
|
35.1
|
1.0
|
|
HD11
|
B:ILE51
|
4.5
|
35.0
|
1.0
|
|
N
|
B:ARG50
|
4.5
|
31.1
|
1.0
|
|
CA
|
B:ARG50
|
4.5
|
31.3
|
1.0
|
|
CA
|
B:ILE49
|
4.5
|
31.9
|
1.0
|
|
HD23
|
B:LEU45
|
4.6
|
41.4
|
1.0
|
|
CA
|
B:LEU44
|
4.6
|
30.1
|
1.0
|
|
CB
|
B:SER47
|
4.6
|
37.2
|
1.0
|
|
HA
|
B:SER48
|
4.7
|
43.0
|
1.0
|
|
HB
|
B:ILE49
|
4.7
|
37.1
|
1.0
|
|
N
|
B:SER48
|
4.7
|
35.5
|
1.0
|
|
HA
|
B:LEU44
|
4.7
|
36.2
|
1.0
|
|
CG1
|
B:ILE51
|
4.8
|
28.1
|
1.0
|
|
CB
|
B:LEU44
|
4.8
|
30.8
|
1.0
|
|
O
|
B:SER48
|
4.8
|
35.4
|
1.0
|
|
N
|
B:ILE51
|
4.9
|
29.1
|
1.0
|
|
CA
|
B:SER48
|
4.9
|
35.9
|
1.0
|
|
HD12
|
B:ILE51
|
4.9
|
35.0
|
1.0
|
|
CD1
|
B:ILE51
|
4.9
|
29.2
|
1.0
|
|
N
|
B:ASP46
|
5.0
|
35.9
|
1.0
|
|
H
|
B:LEU45
|
5.0
|
41.1
|
1.0
|
|
Reference:
A.J.Latta,
F.H.Andrews,
M.J.Mcleish.
Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor To Be Published.
Page generated: Tue Aug 12 21:22:41 2025
|
