Potassium in PDB 5uuz: Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200
Enzymatic activity of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200
All present enzymatic activity of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200:
1.1.1.205;
Protein crystallography data
The structure of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200, PDB code: 5uuz
was solved by
Y.Kim,
N.Maltseva,
R.Mulligan,
M.Makowska-Grzyska,
M.Gu,
D.Gollapalli,
L.Hedstrom,
W.F.Anderson,
A.Joachimiak,
Center For Structural Genomicsof Infectious Diseases (Csgid),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
40.75 /
2.50
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
82.818,
89.887,
104.620,
99.27,
89.94,
96.15
|
R / Rfree (%)
|
22.3 /
25.5
|
Other elements in 5uuz:
The structure of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200 also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200
(pdb code 5uuz). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 8 binding sites of Potassium where determined in the
Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200, PDB code: 5uuz:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 5uuz
Go back to
Potassium Binding Sites List in 5uuz
Potassium binding site 1 out
of 8 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K503
b:52.5
occ:1.00
|
O
|
A:SER471
|
2.7
|
35.0
|
1.0
|
O
|
A:GLU470
|
2.7
|
28.4
|
1.0
|
O
|
B:GLY305
|
2.8
|
30.8
|
1.0
|
O
|
B:CYS308
|
2.8
|
24.6
|
1.0
|
O
|
A:HIS472
|
2.9
|
32.9
|
1.0
|
O
|
B:GLY303
|
3.0
|
39.2
|
1.0
|
C
|
A:SER471
|
3.2
|
33.1
|
1.0
|
C
|
A:HIS472
|
3.3
|
32.7
|
1.0
|
C
|
B:CYS308
|
3.8
|
25.4
|
1.0
|
C
|
A:GLU470
|
3.8
|
29.7
|
1.0
|
N
|
A:HIS472
|
3.8
|
33.1
|
1.0
|
N
|
A:PRO473
|
3.9
|
34.8
|
1.0
|
CA
|
A:SER471
|
3.9
|
31.4
|
1.0
|
C
|
B:GLY305
|
3.9
|
32.0
|
1.0
|
CB
|
B:CYS308
|
4.0
|
29.8
|
1.0
|
CA
|
A:HIS472
|
4.0
|
32.0
|
1.0
|
C
|
B:PRO304
|
4.1
|
31.1
|
1.0
|
O
|
B:PRO304
|
4.1
|
31.1
|
1.0
|
C
|
B:GLY303
|
4.2
|
35.5
|
1.0
|
CA
|
B:CYS308
|
4.2
|
26.9
|
1.0
|
N
|
B:CYS308
|
4.2
|
24.8
|
1.0
|
CA
|
A:PRO473
|
4.2
|
36.0
|
1.0
|
N
|
B:GLY305
|
4.3
|
30.9
|
1.0
|
CD2
|
A:HIS474
|
4.3
|
37.1
|
1.0
|
N
|
A:SER471
|
4.3
|
28.6
|
1.0
|
CA
|
B:PRO304
|
4.5
|
31.6
|
1.0
|
SG
|
B:CYS308
|
4.6
|
34.5
|
1.0
|
NE2
|
A:HIS474
|
4.6
|
36.8
|
1.0
|
CD
|
A:PRO473
|
4.7
|
35.4
|
1.0
|
CA
|
B:GLY305
|
4.7
|
31.7
|
1.0
|
N
|
B:THR309
|
4.8
|
25.6
|
1.0
|
N
|
B:PRO304
|
4.9
|
33.3
|
1.0
|
N
|
B:SER306
|
5.0
|
31.0
|
1.0
|
|
Potassium binding site 2 out
of 8 in 5uuz
Go back to
Potassium Binding Sites List in 5uuz
Potassium binding site 2 out
of 8 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K504
b:52.5
occ:1.00
|
O
|
C:GLU470
|
2.6
|
34.9
|
1.0
|
O
|
A:GLY305
|
2.7
|
29.2
|
1.0
|
O
|
C:SER471
|
2.8
|
37.2
|
1.0
|
O
|
A:CYS308
|
2.9
|
19.8
|
1.0
|
O
|
C:HIS472
|
2.9
|
28.8
|
1.0
|
O
|
A:GLY303
|
2.9
|
26.5
|
1.0
|
C
|
C:SER471
|
3.3
|
32.8
|
1.0
|
C
|
C:HIS472
|
3.4
|
28.6
|
1.0
|
C
|
C:GLU470
|
3.8
|
31.4
|
1.0
|
C
|
A:CYS308
|
3.8
|
22.2
|
1.0
|
C
|
A:GLY305
|
3.9
|
27.9
|
1.0
|
N
|
C:HIS472
|
3.9
|
30.0
|
1.0
|
CB
|
A:CYS308
|
3.9
|
27.2
|
1.0
|
CA
|
C:SER471
|
3.9
|
31.8
|
1.0
|
N
|
C:PRO473
|
4.0
|
26.9
|
1.0
|
C
|
A:PRO304
|
4.0
|
28.1
|
1.0
|
C
|
A:GLY303
|
4.1
|
28.4
|
1.0
|
CA
|
C:HIS472
|
4.1
|
29.1
|
1.0
|
O
|
A:PRO304
|
4.2
|
29.8
|
1.0
|
N
|
A:GLY305
|
4.2
|
25.1
|
1.0
|
CA
|
A:CYS308
|
4.2
|
26.1
|
1.0
|
N
|
A:CYS308
|
4.3
|
28.2
|
1.0
|
CD2
|
C:HIS474
|
4.3
|
32.5
|
1.0
|
N
|
C:SER471
|
4.3
|
29.7
|
1.0
|
CA
|
C:PRO473
|
4.3
|
28.1
|
1.0
|
SG
|
A:CYS308
|
4.5
|
33.2
|
1.0
|
CA
|
A:PRO304
|
4.5
|
27.4
|
1.0
|
NE2
|
C:HIS474
|
4.5
|
33.4
|
1.0
|
CA
|
A:GLY305
|
4.6
|
26.1
|
1.0
|
N
|
A:PRO304
|
4.8
|
27.8
|
1.0
|
N
|
A:THR309
|
4.9
|
21.6
|
1.0
|
CD
|
C:PRO473
|
4.9
|
23.3
|
1.0
|
N
|
A:SER306
|
4.9
|
25.8
|
1.0
|
CA
|
C:GLU470
|
5.0
|
30.7
|
1.0
|
|
Potassium binding site 3 out
of 8 in 5uuz
Go back to
Potassium Binding Sites List in 5uuz
Potassium binding site 3 out
of 8 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K502
b:52.5
occ:1.00
|
O
|
D:GLY305
|
2.6
|
29.8
|
1.0
|
O
|
B:GLU470
|
2.7
|
41.4
|
1.0
|
O
|
B:SER471
|
2.8
|
42.5
|
1.0
|
O
|
D:GLY303
|
2.9
|
24.0
|
1.0
|
O
|
D:CYS308
|
3.0
|
30.2
|
1.0
|
O
|
B:HIS472
|
3.1
|
34.9
|
1.0
|
C
|
B:SER471
|
3.4
|
39.3
|
1.0
|
C
|
B:HIS472
|
3.5
|
35.7
|
1.0
|
C
|
D:GLY305
|
3.8
|
28.3
|
1.0
|
C
|
D:CYS308
|
3.9
|
31.5
|
1.0
|
C
|
D:PRO304
|
3.9
|
22.8
|
1.0
|
C
|
B:GLU470
|
3.9
|
40.3
|
1.0
|
CB
|
D:CYS308
|
3.9
|
33.8
|
1.0
|
O
|
D:PRO304
|
4.0
|
19.2
|
1.0
|
N
|
B:PRO473
|
4.0
|
37.1
|
1.0
|
CA
|
B:SER471
|
4.0
|
38.7
|
1.0
|
N
|
D:GLY305
|
4.0
|
23.9
|
1.0
|
C
|
D:GLY303
|
4.0
|
23.8
|
1.0
|
N
|
B:HIS472
|
4.1
|
37.2
|
1.0
|
CD2
|
B:HIS474
|
4.2
|
33.0
|
1.0
|
CA
|
D:CYS308
|
4.2
|
32.7
|
1.0
|
N
|
D:CYS308
|
4.2
|
31.0
|
1.0
|
CA
|
B:PRO473
|
4.2
|
36.8
|
1.0
|
CA
|
B:HIS472
|
4.3
|
35.8
|
1.0
|
CA
|
D:PRO304
|
4.4
|
22.9
|
1.0
|
NE2
|
B:HIS474
|
4.4
|
33.9
|
1.0
|
N
|
B:SER471
|
4.4
|
39.2
|
1.0
|
CA
|
D:GLY305
|
4.5
|
26.7
|
1.0
|
SG
|
D:CYS308
|
4.5
|
36.5
|
1.0
|
N
|
D:PRO304
|
4.7
|
24.2
|
1.0
|
N
|
D:SER306
|
4.8
|
29.2
|
1.0
|
CD
|
B:PRO473
|
4.8
|
36.6
|
1.0
|
CA
|
D:SER306
|
5.0
|
29.6
|
1.0
|
C
|
D:SER306
|
5.0
|
31.8
|
1.0
|
N
|
D:THR309
|
5.0
|
31.5
|
1.0
|
|
Potassium binding site 4 out
of 8 in 5uuz
Go back to
Potassium Binding Sites List in 5uuz
Potassium binding site 4 out
of 8 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K503
b:74.6
occ:1.00
|
O
|
C:CYS308
|
2.7
|
22.1
|
1.0
|
O
|
C:GLY305
|
2.7
|
30.4
|
1.0
|
O
|
D:SER471
|
2.7
|
43.9
|
1.0
|
O
|
D:GLU470
|
2.9
|
40.8
|
1.0
|
O
|
D:HIS472
|
3.0
|
35.0
|
1.0
|
O
|
C:GLY303
|
3.1
|
24.9
|
1.0
|
C
|
D:SER471
|
3.3
|
38.8
|
1.0
|
C
|
D:HIS472
|
3.4
|
34.5
|
1.0
|
C
|
C:CYS308
|
3.6
|
21.2
|
1.0
|
N
|
D:PRO473
|
3.8
|
35.0
|
1.0
|
C
|
C:GLY305
|
3.8
|
29.2
|
1.0
|
CB
|
C:CYS308
|
3.9
|
26.0
|
1.0
|
N
|
D:HIS472
|
4.0
|
33.7
|
1.0
|
C
|
D:GLU470
|
4.0
|
38.7
|
1.0
|
CA
|
D:SER471
|
4.0
|
38.3
|
1.0
|
CA
|
C:CYS308
|
4.1
|
24.4
|
1.0
|
CA
|
D:HIS472
|
4.1
|
33.4
|
1.0
|
CA
|
D:PRO473
|
4.1
|
35.1
|
1.0
|
C
|
C:PRO304
|
4.1
|
27.5
|
1.0
|
N
|
C:CYS308
|
4.1
|
24.6
|
1.0
|
N
|
C:GLY305
|
4.2
|
27.9
|
1.0
|
O
|
C:PRO304
|
4.2
|
27.5
|
1.0
|
C
|
C:GLY303
|
4.3
|
24.9
|
1.0
|
SG
|
C:CYS308
|
4.4
|
30.1
|
1.0
|
ND1
|
D:HIS474
|
4.5
|
35.8
|
1.0
|
N
|
D:SER471
|
4.5
|
38.4
|
1.0
|
CD
|
D:PRO473
|
4.5
|
36.9
|
1.0
|
CE1
|
D:HIS474
|
4.6
|
36.2
|
1.0
|
CA
|
C:GLY305
|
4.6
|
28.6
|
1.0
|
CA
|
C:PRO304
|
4.7
|
26.8
|
1.0
|
N
|
C:THR309
|
4.7
|
20.3
|
1.0
|
N
|
C:SER306
|
4.9
|
28.3
|
1.0
|
N
|
C:PRO304
|
4.9
|
26.4
|
1.0
|
|
Potassium binding site 5 out
of 8 in 5uuz
Go back to
Potassium Binding Sites List in 5uuz
Potassium binding site 5 out
of 8 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K503
b:95.6
occ:1.00
|
O
|
E:SER471
|
2.6
|
43.2
|
1.0
|
O
|
F:CYS308
|
2.7
|
24.6
|
1.0
|
O
|
E:GLU470
|
2.7
|
42.7
|
1.0
|
O
|
F:GLY303
|
2.9
|
35.7
|
1.0
|
O
|
F:GLY305
|
2.9
|
35.0
|
1.0
|
O
|
E:HIS472
|
3.0
|
37.7
|
1.0
|
C
|
E:SER471
|
3.1
|
40.4
|
1.0
|
C
|
E:HIS472
|
3.4
|
37.4
|
1.0
|
C
|
F:CYS308
|
3.7
|
26.1
|
1.0
|
CA
|
E:SER471
|
3.8
|
40.3
|
1.0
|
C
|
E:GLU470
|
3.8
|
40.2
|
1.0
|
N
|
E:HIS472
|
3.9
|
39.1
|
1.0
|
CB
|
F:CYS308
|
3.9
|
30.0
|
1.0
|
N
|
E:PRO473
|
4.0
|
37.0
|
1.0
|
C
|
F:GLY303
|
4.0
|
34.9
|
1.0
|
C
|
F:GLY305
|
4.0
|
32.6
|
1.0
|
CA
|
E:HIS472
|
4.1
|
38.2
|
1.0
|
CA
|
F:CYS308
|
4.1
|
29.9
|
1.0
|
C
|
F:PRO304
|
4.2
|
31.8
|
1.0
|
N
|
F:CYS308
|
4.3
|
31.4
|
1.0
|
N
|
F:GLY305
|
4.3
|
31.2
|
1.0
|
N
|
E:SER471
|
4.3
|
38.8
|
1.0
|
SG
|
F:CYS308
|
4.3
|
33.0
|
1.0
|
O
|
F:PRO304
|
4.4
|
32.7
|
1.0
|
CA
|
E:PRO473
|
4.4
|
36.6
|
1.0
|
ND1
|
E:HIS474
|
4.4
|
34.7
|
1.0
|
CE1
|
E:HIS474
|
4.5
|
34.2
|
1.0
|
CA
|
F:PRO304
|
4.6
|
32.0
|
1.0
|
N
|
F:THR309
|
4.7
|
24.9
|
1.0
|
CA
|
F:GLY305
|
4.8
|
32.1
|
1.0
|
N
|
F:PRO304
|
4.8
|
33.9
|
1.0
|
CD
|
E:PRO473
|
4.8
|
35.7
|
1.0
|
CA
|
F:GLY303
|
4.9
|
37.9
|
1.0
|
|
Potassium binding site 6 out
of 8 in 5uuz
Go back to
Potassium Binding Sites List in 5uuz
Potassium binding site 6 out
of 8 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K504
b:52.5
occ:1.00
|
O
|
E:GLY305
|
2.6
|
32.7
|
1.0
|
O
|
E:CYS308
|
2.7
|
28.8
|
1.0
|
O
|
G:SER471
|
2.7
|
40.4
|
1.0
|
O
|
E:GLY303
|
2.9
|
23.1
|
1.0
|
O
|
G:GLU470
|
3.0
|
34.2
|
1.0
|
O
|
G:HIS472
|
3.1
|
35.8
|
1.0
|
C
|
G:SER471
|
3.4
|
36.1
|
1.0
|
C
|
G:HIS472
|
3.5
|
35.5
|
1.0
|
C
|
E:CYS308
|
3.6
|
27.3
|
1.0
|
CB
|
E:CYS308
|
3.8
|
30.8
|
1.0
|
C
|
E:GLY305
|
3.8
|
33.4
|
1.0
|
N
|
G:PRO473
|
3.9
|
36.6
|
1.0
|
C
|
E:PRO304
|
4.0
|
28.2
|
1.0
|
CA
|
E:CYS308
|
4.0
|
28.5
|
1.0
|
CA
|
G:SER471
|
4.0
|
33.6
|
1.0
|
N
|
E:CYS308
|
4.1
|
26.7
|
1.0
|
N
|
G:HIS472
|
4.1
|
34.5
|
1.0
|
C
|
G:GLU470
|
4.1
|
34.6
|
1.0
|
C
|
E:GLY303
|
4.1
|
23.7
|
1.0
|
N
|
E:GLY305
|
4.1
|
29.5
|
1.0
|
O
|
E:PRO304
|
4.2
|
31.4
|
1.0
|
CA
|
G:PRO473
|
4.2
|
36.5
|
1.0
|
CA
|
G:HIS472
|
4.2
|
35.4
|
1.0
|
CD2
|
G:HIS474
|
4.3
|
34.5
|
1.0
|
SG
|
E:CYS308
|
4.4
|
34.1
|
1.0
|
CA
|
E:PRO304
|
4.5
|
25.9
|
1.0
|
CA
|
E:GLY305
|
4.5
|
33.1
|
1.0
|
NE2
|
G:HIS474
|
4.5
|
34.9
|
1.0
|
N
|
G:SER471
|
4.5
|
34.5
|
1.0
|
N
|
E:THR309
|
4.7
|
25.7
|
1.0
|
CD
|
G:PRO473
|
4.8
|
36.5
|
1.0
|
N
|
E:PRO304
|
4.8
|
25.4
|
1.0
|
N
|
E:SER306
|
4.9
|
32.4
|
1.0
|
C
|
E:SER306
|
5.0
|
27.3
|
1.0
|
|
Potassium binding site 7 out
of 8 in 5uuz
Go back to
Potassium Binding Sites List in 5uuz
Potassium binding site 7 out
of 8 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 7 of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K502
b:93.3
occ:1.00
|
O
|
F:GLU470
|
2.5
|
47.7
|
1.0
|
O
|
F:SER471
|
2.7
|
50.0
|
1.0
|
O
|
H:GLY305
|
2.8
|
38.7
|
1.0
|
O
|
H:GLY303
|
2.8
|
45.8
|
1.0
|
O
|
F:HIS472
|
3.0
|
39.6
|
1.0
|
O
|
H:CYS308
|
3.1
|
37.9
|
1.0
|
C
|
F:SER471
|
3.1
|
45.6
|
1.0
|
C
|
F:HIS472
|
3.4
|
40.5
|
1.0
|
C
|
F:GLU470
|
3.6
|
45.2
|
1.0
|
CA
|
F:SER471
|
3.8
|
44.5
|
1.0
|
N
|
F:HIS472
|
3.8
|
44.2
|
1.0
|
C
|
H:GLY305
|
3.9
|
37.8
|
1.0
|
C
|
H:PRO304
|
3.9
|
41.2
|
1.0
|
C
|
H:CYS308
|
4.0
|
37.4
|
1.0
|
N
|
F:PRO473
|
4.0
|
40.9
|
1.0
|
C
|
H:GLY303
|
4.0
|
41.8
|
1.0
|
O
|
H:PRO304
|
4.0
|
42.7
|
1.0
|
CB
|
H:CYS308
|
4.1
|
38.6
|
1.0
|
CA
|
F:HIS472
|
4.1
|
42.3
|
1.0
|
N
|
H:GLY305
|
4.1
|
39.6
|
1.0
|
N
|
F:SER471
|
4.2
|
44.8
|
1.0
|
CD2
|
F:HIS474
|
4.2
|
46.4
|
1.0
|
CA
|
H:PRO304
|
4.3
|
41.3
|
1.0
|
CA
|
F:PRO473
|
4.3
|
39.8
|
1.0
|
CA
|
H:CYS308
|
4.4
|
37.7
|
1.0
|
N
|
H:CYS308
|
4.5
|
35.5
|
1.0
|
NE2
|
F:HIS474
|
4.5
|
46.6
|
1.0
|
SG
|
H:CYS308
|
4.6
|
41.6
|
1.0
|
CA
|
H:GLY305
|
4.6
|
38.3
|
1.0
|
N
|
H:PRO304
|
4.7
|
41.5
|
1.0
|
CD
|
F:PRO473
|
4.8
|
41.4
|
1.0
|
CA
|
F:GLU470
|
4.8
|
43.7
|
1.0
|
N
|
H:SER306
|
5.0
|
36.2
|
1.0
|
|
Potassium binding site 8 out
of 8 in 5uuz
Go back to
Potassium Binding Sites List in 5uuz
Potassium binding site 8 out
of 8 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 8 of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:K503
b:83.8
occ:1.00
|
O
|
H:SER471
|
2.6
|
35.8
|
1.0
|
O
|
H:GLU470
|
2.7
|
38.4
|
1.0
|
O
|
G:GLY303
|
2.8
|
31.0
|
1.0
|
O
|
G:GLY305
|
2.8
|
33.7
|
1.0
|
O
|
G:CYS308
|
2.9
|
32.3
|
1.0
|
O
|
H:HIS472
|
3.1
|
33.7
|
1.0
|
O
|
H:HOH609
|
3.1
|
16.5
|
1.0
|
C
|
H:SER471
|
3.2
|
34.4
|
1.0
|
C
|
H:HIS472
|
3.5
|
35.0
|
1.0
|
C
|
H:GLU470
|
3.8
|
37.2
|
1.0
|
C
|
G:CYS308
|
3.8
|
34.4
|
1.0
|
CA
|
H:SER471
|
3.8
|
34.2
|
1.0
|
CB
|
G:CYS308
|
3.9
|
35.9
|
1.0
|
C
|
G:GLY303
|
3.9
|
32.0
|
1.0
|
N
|
H:HIS472
|
4.0
|
33.4
|
1.0
|
C
|
G:GLY305
|
4.0
|
32.7
|
1.0
|
C
|
G:PRO304
|
4.0
|
29.7
|
1.0
|
N
|
H:PRO473
|
4.0
|
38.2
|
1.0
|
O
|
G:PRO304
|
4.2
|
28.0
|
1.0
|
N
|
G:GLY305
|
4.2
|
30.6
|
1.0
|
CA
|
H:HIS472
|
4.2
|
35.1
|
1.0
|
CA
|
G:CYS308
|
4.2
|
36.7
|
1.0
|
N
|
H:SER471
|
4.3
|
34.8
|
1.0
|
N
|
G:CYS308
|
4.3
|
37.9
|
1.0
|
CA
|
G:PRO304
|
4.4
|
31.3
|
1.0
|
CA
|
H:PRO473
|
4.4
|
40.3
|
1.0
|
SG
|
G:CYS308
|
4.4
|
36.4
|
1.0
|
ND1
|
H:HIS474
|
4.4
|
41.6
|
1.0
|
CE1
|
H:HIS474
|
4.4
|
42.1
|
1.0
|
N
|
G:PRO304
|
4.7
|
31.8
|
1.0
|
CA
|
G:GLY305
|
4.7
|
32.2
|
1.0
|
CD
|
H:PRO473
|
4.9
|
39.3
|
1.0
|
N
|
G:THR309
|
4.9
|
35.1
|
1.0
|
CA
|
G:GLY303
|
4.9
|
35.0
|
1.0
|
|
Reference:
Y.Kim,
N.Maltseva,
R.Mulligan,
M.Makowska-Grzyska,
M.Gu,
D.Gollapalli,
L.Hedstrom,
W.F.Anderson,
A.Joachimiak,
Center For Structural Genomics Of Infectious Diseases(Csgid).
Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P200 To Be Published.
Page generated: Mon Aug 12 14:43:48 2024
|