Potassium in PDB 5urs: Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P178
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 P178
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 P178:
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 P178, PDB code: 5urs
was solved by
Y.Kim,
N.Maltseva,
M.Makowska-Grzyska,
M.Gu,
D.Gollapalli,
L.Hedstrom,
W.F.Anderson,
A.Joachimiak,
Center For Structural Genomics Ofinfectious Diseases (Csgid),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
42.86 /
2.39
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
85.345,
89.581,
104.158,
98.71,
89.82,
96.69
|
R / Rfree (%)
|
22.4 /
27.9
|
Other elements in 5urs:
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 P178 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 P178
(pdb code 5urs). 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 P178, PDB code: 5urs:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 5urs
Go back to
Potassium Binding Sites List in 5urs
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 P178
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 P178 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K503
b:40.5
occ:1.00
|
O
|
B:GLY303
|
2.8
|
28.2
|
1.0
|
O
|
B:GLY305
|
2.8
|
36.4
|
1.0
|
O
|
A:SER471
|
2.8
|
35.2
|
1.0
|
O
|
A:GLU470
|
2.8
|
40.9
|
1.0
|
O
|
A:HIS472
|
2.9
|
32.0
|
1.0
|
O
|
B:CYS308
|
2.9
|
28.6
|
1.0
|
C
|
A:SER471
|
3.3
|
32.5
|
1.0
|
O
|
B:HOH610
|
3.5
|
36.0
|
1.0
|
C
|
A:HIS472
|
3.5
|
33.6
|
1.0
|
C
|
B:CYS308
|
3.8
|
31.1
|
1.0
|
CB
|
B:CYS308
|
3.8
|
30.4
|
1.0
|
C
|
B:PRO304
|
3.8
|
33.9
|
1.0
|
C
|
B:GLY305
|
3.9
|
34.4
|
1.0
|
C
|
B:GLY303
|
4.0
|
27.6
|
1.0
|
CA
|
A:SER471
|
4.0
|
30.0
|
1.0
|
C
|
A:GLU470
|
4.0
|
33.8
|
1.0
|
O
|
B:PRO304
|
4.0
|
34.0
|
1.0
|
N
|
A:HIS472
|
4.0
|
31.6
|
1.0
|
N
|
B:GLY305
|
4.1
|
22.1
|
1.0
|
N
|
A:PRO473
|
4.1
|
29.1
|
1.0
|
CA
|
B:CYS308
|
4.1
|
30.4
|
1.0
|
CD2
|
A:HIS474
|
4.1
|
22.2
|
1.0
|
N
|
B:CYS308
|
4.2
|
26.1
|
1.0
|
CA
|
B:PRO304
|
4.2
|
28.9
|
1.0
|
CA
|
A:HIS472
|
4.3
|
31.5
|
1.0
|
SG
|
B:CYS308
|
4.3
|
37.8
|
1.0
|
CA
|
A:PRO473
|
4.4
|
24.9
|
1.0
|
NE2
|
A:HIS474
|
4.4
|
26.6
|
1.0
|
N
|
A:SER471
|
4.4
|
27.8
|
1.0
|
CA
|
B:GLY305
|
4.6
|
29.1
|
1.0
|
N
|
B:PRO304
|
4.6
|
27.7
|
1.0
|
N
|
B:THR309
|
4.9
|
31.4
|
1.0
|
O
|
B:SER306
|
5.0
|
24.5
|
1.0
|
N
|
B:SER306
|
5.0
|
33.0
|
1.0
|
|
Potassium binding site 2 out
of 8 in 5urs
Go back to
Potassium Binding Sites List in 5urs
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 P178
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 P178 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K505
b:37.9
occ:1.00
|
O
|
A:GLY303
|
2.7
|
35.1
|
1.0
|
O
|
C:SER471
|
2.8
|
28.7
|
1.0
|
O
|
C:GLU470
|
2.8
|
33.3
|
1.0
|
O
|
A:GLY305
|
2.9
|
28.1
|
1.0
|
O
|
A:CYS308
|
2.9
|
27.7
|
1.0
|
O
|
C:HIS472
|
3.0
|
25.4
|
1.0
|
C
|
C:SER471
|
3.4
|
31.9
|
1.0
|
O
|
A:HOH615
|
3.5
|
27.6
|
1.0
|
C
|
C:HIS472
|
3.6
|
31.6
|
1.0
|
C
|
A:PRO304
|
3.7
|
31.5
|
1.0
|
O
|
A:PRO304
|
3.8
|
26.1
|
1.0
|
C
|
A:CYS308
|
3.8
|
26.2
|
1.0
|
C
|
A:GLY303
|
3.9
|
31.9
|
1.0
|
C
|
A:GLY305
|
3.9
|
28.3
|
1.0
|
CB
|
A:CYS308
|
3.9
|
23.3
|
1.0
|
C
|
C:GLU470
|
3.9
|
30.6
|
1.0
|
N
|
A:GLY305
|
3.9
|
34.2
|
1.0
|
CA
|
C:SER471
|
4.0
|
32.2
|
1.0
|
CA
|
A:PRO304
|
4.1
|
30.8
|
1.0
|
N
|
C:PRO473
|
4.2
|
37.7
|
1.0
|
N
|
C:HIS472
|
4.2
|
37.7
|
1.0
|
CA
|
A:CYS308
|
4.2
|
25.7
|
1.0
|
N
|
A:CYS308
|
4.3
|
29.9
|
1.0
|
CD2
|
C:HIS474
|
4.4
|
30.3
|
1.0
|
CA
|
C:HIS472
|
4.4
|
34.6
|
1.0
|
CA
|
C:PRO473
|
4.4
|
35.5
|
1.0
|
SG
|
A:CYS308
|
4.4
|
21.0
|
1.0
|
N
|
C:SER471
|
4.5
|
29.9
|
1.0
|
N
|
A:PRO304
|
4.5
|
29.5
|
1.0
|
CA
|
A:GLY305
|
4.5
|
20.0
|
1.0
|
NE2
|
C:HIS474
|
4.7
|
32.4
|
1.0
|
N
|
A:THR309
|
4.9
|
23.1
|
1.0
|
CA
|
A:GLY303
|
4.9
|
33.6
|
1.0
|
N
|
A:SER306
|
5.0
|
27.3
|
1.0
|
|
Potassium binding site 3 out
of 8 in 5urs
Go back to
Potassium Binding Sites List in 5urs
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 P178
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 P178 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K502
b:37.6
occ:1.00
|
O
|
D:GLY305
|
2.7
|
29.5
|
1.0
|
O
|
B:GLU470
|
2.8
|
25.3
|
1.0
|
O
|
B:HIS472
|
2.9
|
33.2
|
1.0
|
O
|
D:CYS308
|
2.9
|
25.6
|
1.0
|
O
|
D:GLY303
|
3.0
|
38.6
|
1.0
|
O
|
B:SER471
|
3.0
|
25.6
|
1.0
|
C
|
B:SER471
|
3.4
|
25.9
|
1.0
|
O
|
B:HOH623
|
3.5
|
32.2
|
1.0
|
C
|
B:HIS472
|
3.5
|
32.9
|
1.0
|
O
|
D:PRO304
|
3.6
|
36.0
|
1.0
|
C
|
D:PRO304
|
3.6
|
32.6
|
1.0
|
C
|
D:GLY305
|
3.8
|
27.6
|
1.0
|
N
|
D:GLY305
|
3.8
|
29.3
|
1.0
|
C
|
B:GLU470
|
3.9
|
32.9
|
1.0
|
C
|
D:CYS308
|
3.9
|
24.8
|
1.0
|
CA
|
B:SER471
|
3.9
|
31.7
|
1.0
|
C
|
D:GLY303
|
4.0
|
28.0
|
1.0
|
CB
|
D:CYS308
|
4.1
|
32.0
|
1.0
|
N
|
B:PRO473
|
4.1
|
34.8
|
1.0
|
N
|
B:HIS472
|
4.1
|
25.7
|
1.0
|
CA
|
D:PRO304
|
4.2
|
29.8
|
1.0
|
N
|
B:SER471
|
4.3
|
33.0
|
1.0
|
CA
|
D:GLY305
|
4.3
|
27.5
|
1.0
|
CA
|
D:CYS308
|
4.3
|
26.1
|
1.0
|
CA
|
B:HIS472
|
4.3
|
30.6
|
1.0
|
CA
|
B:PRO473
|
4.3
|
34.2
|
1.0
|
N
|
D:CYS308
|
4.4
|
27.1
|
1.0
|
CD2
|
B:HIS474
|
4.4
|
33.7
|
1.0
|
SG
|
D:CYS308
|
4.5
|
37.6
|
1.0
|
N
|
D:PRO304
|
4.6
|
26.3
|
1.0
|
NE2
|
B:HIS474
|
4.8
|
34.0
|
1.0
|
N
|
D:SER306
|
4.9
|
23.9
|
1.0
|
N
|
D:THR309
|
5.0
|
26.2
|
1.0
|
|
Potassium binding site 4 out
of 8 in 5urs
Go back to
Potassium Binding Sites List in 5urs
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 P178
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 P178 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K505
b:39.7
occ:1.00
|
O
|
C:GLY305
|
2.7
|
34.2
|
1.0
|
O
|
D:GLU470
|
2.7
|
28.4
|
1.0
|
O
|
D:SER471
|
2.8
|
26.9
|
1.0
|
O
|
C:GLY303
|
2.8
|
34.0
|
1.0
|
O
|
C:CYS308
|
3.0
|
27.2
|
1.0
|
O
|
D:HIS472
|
3.0
|
34.5
|
1.0
|
O
|
D:HOH619
|
3.2
|
37.1
|
1.0
|
C
|
D:SER471
|
3.3
|
26.1
|
1.0
|
C
|
D:HIS472
|
3.5
|
36.0
|
1.0
|
C
|
C:CYS308
|
3.8
|
29.5
|
1.0
|
C
|
C:GLY305
|
3.8
|
33.8
|
1.0
|
CA
|
D:SER471
|
3.8
|
23.4
|
1.0
|
C
|
D:GLU470
|
3.8
|
31.6
|
1.0
|
C
|
C:PRO304
|
3.9
|
27.2
|
1.0
|
CB
|
C:CYS308
|
3.9
|
33.2
|
1.0
|
C
|
C:GLY303
|
4.0
|
30.1
|
1.0
|
N
|
C:GLY305
|
4.0
|
30.8
|
1.0
|
N
|
D:PRO473
|
4.0
|
33.1
|
1.0
|
N
|
D:HIS472
|
4.0
|
23.8
|
1.0
|
O
|
C:PRO304
|
4.1
|
26.7
|
1.0
|
CA
|
D:HIS472
|
4.2
|
39.1
|
1.0
|
CA
|
C:CYS308
|
4.3
|
33.7
|
1.0
|
N
|
D:SER471
|
4.3
|
24.3
|
1.0
|
CA
|
D:PRO473
|
4.3
|
33.2
|
1.0
|
N
|
C:CYS308
|
4.3
|
38.5
|
1.0
|
CA
|
C:PRO304
|
4.4
|
27.2
|
1.0
|
SG
|
C:CYS308
|
4.4
|
37.6
|
1.0
|
CD2
|
D:HIS474
|
4.4
|
39.2
|
1.0
|
CA
|
C:GLY305
|
4.5
|
30.1
|
1.0
|
N
|
C:PRO304
|
4.7
|
26.8
|
1.0
|
NE2
|
D:HIS474
|
4.8
|
38.9
|
1.0
|
N
|
C:SER306
|
4.9
|
34.7
|
1.0
|
N
|
C:THR309
|
4.9
|
31.6
|
1.0
|
CD
|
D:PRO473
|
4.9
|
27.1
|
1.0
|
CA
|
C:GLY303
|
5.0
|
28.1
|
1.0
|
|
Potassium binding site 5 out
of 8 in 5urs
Go back to
Potassium Binding Sites List in 5urs
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 P178
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 P178 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K503
b:38.2
occ:1.00
|
O
|
F:GLY303
|
2.6
|
32.7
|
1.0
|
O
|
E:GLU470
|
2.8
|
32.4
|
1.0
|
O
|
F:GLY305
|
2.8
|
32.5
|
1.0
|
O
|
E:SER471
|
2.9
|
24.8
|
1.0
|
O
|
F:CYS308
|
3.1
|
26.6
|
1.0
|
O
|
E:HIS472
|
3.4
|
36.1
|
1.0
|
C
|
E:SER471
|
3.5
|
26.7
|
1.0
|
C
|
F:PRO304
|
3.6
|
31.3
|
1.0
|
O
|
F:PRO304
|
3.7
|
29.8
|
1.0
|
C
|
F:GLY303
|
3.8
|
33.0
|
1.0
|
CB
|
F:CYS308
|
3.8
|
33.5
|
1.0
|
C
|
E:HIS472
|
3.8
|
35.7
|
1.0
|
C
|
F:GLY305
|
3.9
|
34.3
|
1.0
|
N
|
F:GLY305
|
3.9
|
29.4
|
1.0
|
C
|
F:CYS308
|
3.9
|
25.6
|
1.0
|
C
|
E:GLU470
|
3.9
|
34.1
|
1.0
|
CA
|
E:SER471
|
4.0
|
31.6
|
1.0
|
CA
|
F:PRO304
|
4.0
|
29.2
|
1.0
|
CA
|
F:CYS308
|
4.2
|
28.5
|
1.0
|
CD2
|
E:HIS474
|
4.3
|
40.3
|
1.0
|
N
|
E:HIS472
|
4.3
|
29.6
|
1.0
|
N
|
F:CYS308
|
4.3
|
26.5
|
1.0
|
SG
|
F:CYS308
|
4.3
|
42.0
|
1.0
|
N
|
E:PRO473
|
4.3
|
40.6
|
1.0
|
N
|
F:PRO304
|
4.4
|
27.0
|
1.0
|
N
|
E:SER471
|
4.4
|
32.4
|
1.0
|
CA
|
F:GLY305
|
4.4
|
32.2
|
1.0
|
NE2
|
E:HIS474
|
4.6
|
41.5
|
1.0
|
CA
|
E:HIS472
|
4.6
|
34.2
|
1.0
|
CA
|
E:PRO473
|
4.6
|
40.6
|
1.0
|
CA
|
F:GLY303
|
4.9
|
38.6
|
1.0
|
N
|
F:SER306
|
4.9
|
37.8
|
1.0
|
N
|
F:THR309
|
4.9
|
26.2
|
1.0
|
|
Potassium binding site 6 out
of 8 in 5urs
Go back to
Potassium Binding Sites List in 5urs
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 P178
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 P178 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K506
b:38.1
occ:1.00
|
O
|
G:SER471
|
2.7
|
37.6
|
1.0
|
O
|
G:GLU470
|
2.8
|
28.3
|
1.0
|
O
|
E:GLY303
|
2.8
|
38.1
|
1.0
|
O
|
E:CYS308
|
3.0
|
36.0
|
1.0
|
O
|
G:HIS472
|
3.0
|
29.0
|
1.0
|
O
|
E:GLY305
|
3.1
|
23.2
|
1.0
|
C
|
G:SER471
|
3.2
|
35.3
|
1.0
|
O
|
E:HOH625
|
3.4
|
26.7
|
1.0
|
C
|
G:HIS472
|
3.5
|
30.9
|
1.0
|
C
|
E:CYS308
|
3.8
|
35.4
|
1.0
|
CA
|
G:SER471
|
3.8
|
29.2
|
1.0
|
C
|
G:GLU470
|
3.9
|
29.9
|
1.0
|
CB
|
E:CYS308
|
3.9
|
35.0
|
1.0
|
C
|
E:GLY303
|
3.9
|
33.9
|
1.0
|
N
|
G:HIS472
|
4.0
|
35.4
|
1.0
|
C
|
E:PRO304
|
4.1
|
30.9
|
1.0
|
N
|
G:PRO473
|
4.2
|
32.4
|
1.0
|
C
|
E:GLY305
|
4.2
|
34.0
|
1.0
|
CA
|
G:HIS472
|
4.2
|
32.3
|
1.0
|
CA
|
E:CYS308
|
4.2
|
35.2
|
1.0
|
O
|
E:PRO304
|
4.3
|
29.4
|
1.0
|
N
|
E:CYS308
|
4.3
|
33.2
|
1.0
|
N
|
G:SER471
|
4.3
|
27.4
|
1.0
|
N
|
E:GLY305
|
4.4
|
35.6
|
1.0
|
SG
|
E:CYS308
|
4.4
|
35.4
|
1.0
|
CA
|
E:PRO304
|
4.5
|
32.1
|
1.0
|
CD2
|
G:HIS474
|
4.5
|
35.0
|
1.0
|
CA
|
G:PRO473
|
4.6
|
33.8
|
1.0
|
N
|
E:PRO304
|
4.7
|
32.7
|
1.0
|
N
|
E:THR309
|
4.8
|
34.2
|
1.0
|
NE2
|
G:HIS474
|
4.8
|
35.9
|
1.0
|
CA
|
E:GLY305
|
4.9
|
36.3
|
1.0
|
CA
|
E:GLY303
|
4.9
|
32.0
|
1.0
|
|
Potassium binding site 7 out
of 8 in 5urs
Go back to
Potassium Binding Sites List in 5urs
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 P178
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 P178 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K502
b:38.6
occ:1.00
|
O
|
H:GLY303
|
2.7
|
23.6
|
1.0
|
O
|
F:SER471
|
2.7
|
43.0
|
1.0
|
O
|
F:GLU470
|
2.8
|
42.9
|
1.0
|
O
|
H:GLY305
|
2.8
|
39.1
|
1.0
|
O
|
H:CYS308
|
2.9
|
23.1
|
1.0
|
O
|
F:HIS472
|
3.2
|
40.4
|
1.0
|
C
|
F:SER471
|
3.3
|
41.5
|
1.0
|
O
|
H:HOH616
|
3.4
|
28.1
|
1.0
|
C
|
F:HIS472
|
3.5
|
35.9
|
1.0
|
C
|
H:CYS308
|
3.7
|
27.8
|
1.0
|
C
|
H:PRO304
|
3.8
|
25.7
|
1.0
|
C
|
H:GLY303
|
3.9
|
27.8
|
1.0
|
CB
|
H:CYS308
|
3.9
|
35.7
|
1.0
|
CA
|
F:SER471
|
3.9
|
38.9
|
1.0
|
C
|
H:GLY305
|
3.9
|
38.9
|
1.0
|
C
|
F:GLU470
|
3.9
|
41.4
|
1.0
|
N
|
H:GLY305
|
3.9
|
32.5
|
1.0
|
N
|
F:PRO473
|
4.0
|
37.5
|
1.0
|
O
|
H:PRO304
|
4.0
|
25.9
|
1.0
|
N
|
F:HIS472
|
4.1
|
41.0
|
1.0
|
CA
|
H:PRO304
|
4.1
|
25.9
|
1.0
|
CA
|
H:CYS308
|
4.2
|
32.4
|
1.0
|
CA
|
F:HIS472
|
4.2
|
34.4
|
1.0
|
N
|
H:CYS308
|
4.3
|
35.7
|
1.0
|
CA
|
F:PRO473
|
4.3
|
35.0
|
1.0
|
SG
|
H:CYS308
|
4.3
|
41.8
|
1.0
|
CE1
|
F:HIS474
|
4.3
|
41.0
|
1.0
|
N
|
F:SER471
|
4.4
|
39.4
|
1.0
|
ND1
|
F:HIS474
|
4.4
|
39.6
|
1.0
|
N
|
H:PRO304
|
4.5
|
28.9
|
1.0
|
CA
|
H:GLY305
|
4.5
|
35.0
|
1.0
|
N
|
H:THR309
|
4.8
|
27.0
|
1.0
|
CD
|
F:PRO473
|
4.8
|
38.0
|
1.0
|
CA
|
H:GLY303
|
5.0
|
30.5
|
1.0
|
|
Potassium binding site 8 out
of 8 in 5urs
Go back to
Potassium Binding Sites List in 5urs
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 P178
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 P178 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:K502
b:36.3
occ:1.00
|
O
|
H:SER471
|
2.6
|
29.5
|
1.0
|
O
|
G:GLY305
|
2.8
|
34.5
|
1.0
|
O
|
H:GLU470
|
2.8
|
31.8
|
1.0
|
O
|
H:HIS472
|
2.9
|
34.0
|
1.0
|
O
|
G:CYS308
|
2.9
|
28.7
|
1.0
|
O
|
G:GLY303
|
2.9
|
28.0
|
1.0
|
C
|
H:SER471
|
3.2
|
32.2
|
1.0
|
C
|
H:HIS472
|
3.5
|
37.9
|
1.0
|
O
|
G:HOH608
|
3.6
|
26.4
|
1.0
|
C
|
G:CYS308
|
3.8
|
29.9
|
1.0
|
CA
|
H:SER471
|
3.8
|
35.1
|
1.0
|
C
|
G:PRO304
|
3.8
|
37.4
|
1.0
|
C
|
H:GLU470
|
3.9
|
32.2
|
1.0
|
C
|
G:GLY305
|
3.9
|
36.0
|
1.0
|
CB
|
G:CYS308
|
3.9
|
33.4
|
1.0
|
N
|
H:HIS472
|
3.9
|
34.6
|
1.0
|
O
|
G:PRO304
|
3.9
|
40.2
|
1.0
|
C
|
G:GLY303
|
4.0
|
28.9
|
1.0
|
N
|
G:GLY305
|
4.0
|
36.5
|
1.0
|
CA
|
G:CYS308
|
4.2
|
32.5
|
1.0
|
N
|
H:PRO473
|
4.2
|
40.0
|
1.0
|
CA
|
H:HIS472
|
4.2
|
35.2
|
1.0
|
N
|
G:CYS308
|
4.2
|
33.6
|
1.0
|
CA
|
G:PRO304
|
4.3
|
34.3
|
1.0
|
N
|
H:SER471
|
4.3
|
32.8
|
1.0
|
CD2
|
H:HIS474
|
4.4
|
34.2
|
1.0
|
SG
|
G:CYS308
|
4.4
|
33.7
|
1.0
|
CA
|
G:GLY305
|
4.5
|
35.6
|
1.0
|
CA
|
H:PRO473
|
4.5
|
35.4
|
1.0
|
NE2
|
H:HIS474
|
4.6
|
34.8
|
1.0
|
N
|
G:PRO304
|
4.6
|
27.8
|
1.0
|
N
|
G:THR309
|
4.9
|
29.9
|
1.0
|
N
|
G:SER306
|
5.0
|
33.9
|
1.0
|
|
Reference:
Y.Kim,
N.Maltseva,
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 P178 To Be Published.
Page generated: Mon Aug 12 14:43:32 2024
|