Potassium in PDB 7mtu: Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P221
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 P221
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 P221:
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 P221, PDB code: 7mtu
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)
|
41.68 /
2.34
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
83.27,
89.334,
104.334,
98.89,
90.4,
96.01
|
R / Rfree (%)
|
23.1 /
27.5
|
Other elements in 7mtu:
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 P221 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 P221
(pdb code 7mtu). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 9 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 P221, PDB code: 7mtu:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
Potassium binding site 1 out
of 9 in 7mtu
Go back to
Potassium Binding Sites List in 7mtu
Potassium binding site 1 out
of 9 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P221
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 P221 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K505
b:17.2
occ:1.00
|
O
|
A:GLU470
|
2.7
|
19.3
|
1.0
|
O
|
B:CYS308
|
2.7
|
19.0
|
1.0
|
O
|
B:GLY305
|
2.7
|
21.9
|
1.0
|
O
|
A:SER471
|
2.8
|
24.6
|
1.0
|
O
|
B:GLY303
|
2.9
|
27.6
|
1.0
|
O
|
A:HIS472
|
2.9
|
16.6
|
1.0
|
O
|
B:HOH630
|
3.0
|
15.7
|
1.0
|
C
|
A:SER471
|
3.3
|
23.5
|
1.0
|
C
|
A:HIS472
|
3.6
|
20.3
|
1.0
|
C
|
B:CYS308
|
3.7
|
20.5
|
1.0
|
C
|
A:GLU470
|
3.8
|
20.4
|
1.0
|
CB
|
B:CYS308
|
3.8
|
17.8
|
1.0
|
C
|
B:GLY305
|
3.9
|
19.0
|
1.0
|
CA
|
A:SER471
|
3.9
|
22.1
|
1.0
|
C
|
B:PRO304
|
3.9
|
19.4
|
1.0
|
C
|
B:GLY303
|
4.0
|
21.3
|
1.0
|
N
|
A:HIS472
|
4.0
|
20.5
|
1.0
|
O
|
B:PRO304
|
4.1
|
24.4
|
1.0
|
N
|
B:GLY305
|
4.1
|
20.0
|
1.0
|
CA
|
B:CYS308
|
4.1
|
18.8
|
1.0
|
N
|
A:PRO473
|
4.2
|
24.5
|
1.0
|
N
|
B:CYS308
|
4.2
|
18.7
|
1.0
|
CA
|
A:HIS472
|
4.3
|
22.9
|
1.0
|
N
|
A:SER471
|
4.3
|
21.7
|
1.0
|
CA
|
B:PRO304
|
4.4
|
23.2
|
1.0
|
SG
|
B:CYS308
|
4.4
|
19.5
|
1.0
|
CA
|
A:PRO473
|
4.5
|
27.0
|
1.0
|
CA
|
B:GLY305
|
4.6
|
19.1
|
1.0
|
ND1
|
A:HIS474
|
4.6
|
22.3
|
1.0
|
N
|
B:PRO304
|
4.7
|
20.3
|
1.0
|
CE1
|
A:HIS474
|
4.7
|
27.7
|
1.0
|
N
|
B:THR309
|
4.8
|
22.3
|
1.0
|
N
|
B:SER306
|
4.9
|
20.7
|
1.0
|
CA
|
A:GLU470
|
5.0
|
21.0
|
1.0
|
|
Potassium binding site 2 out
of 9 in 7mtu
Go back to
Potassium Binding Sites List in 7mtu
Potassium binding site 2 out
of 9 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P221
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 P221 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K503
b:29.1
occ:1.00
|
O
|
B:GLU470
|
2.7
|
24.9
|
1.0
|
O
|
D:GLY305
|
2.8
|
30.0
|
1.0
|
O
|
D:GLY303
|
2.8
|
24.5
|
1.0
|
O
|
B:SER471
|
2.9
|
33.8
|
1.0
|
O
|
D:CYS308
|
2.9
|
24.6
|
1.0
|
O
|
B:HIS472
|
3.0
|
24.0
|
1.0
|
O
|
D:HOH605
|
3.2
|
18.1
|
1.0
|
C
|
B:SER471
|
3.3
|
28.4
|
1.0
|
C
|
B:HIS472
|
3.6
|
25.3
|
1.0
|
C
|
D:CYS308
|
3.8
|
23.0
|
1.0
|
C
|
B:GLU470
|
3.8
|
24.6
|
1.0
|
C
|
D:GLY305
|
3.9
|
31.3
|
1.0
|
C
|
D:PRO304
|
3.9
|
26.8
|
1.0
|
CA
|
B:SER471
|
3.9
|
26.4
|
1.0
|
CB
|
D:CYS308
|
4.0
|
26.6
|
1.0
|
C
|
D:GLY303
|
4.0
|
24.4
|
1.0
|
N
|
B:HIS472
|
4.0
|
26.0
|
1.0
|
N
|
D:GLY305
|
4.1
|
28.9
|
1.0
|
O
|
D:PRO304
|
4.1
|
27.4
|
1.0
|
CE1
|
B:HIS474
|
4.2
|
30.9
|
1.0
|
CA
|
D:CYS308
|
4.2
|
31.5
|
1.0
|
N
|
B:PRO473
|
4.2
|
32.1
|
1.0
|
N
|
D:CYS308
|
4.3
|
29.7
|
1.0
|
CA
|
D:PRO304
|
4.3
|
28.4
|
1.0
|
CA
|
B:HIS472
|
4.3
|
27.2
|
1.0
|
ND1
|
B:HIS474
|
4.3
|
32.5
|
1.0
|
N
|
B:SER471
|
4.3
|
25.6
|
1.0
|
SG
|
D:CYS308
|
4.5
|
30.7
|
1.0
|
CA
|
B:PRO473
|
4.6
|
32.1
|
1.0
|
CA
|
D:GLY305
|
4.6
|
25.4
|
1.0
|
N
|
D:PRO304
|
4.7
|
23.7
|
1.0
|
N
|
D:THR309
|
4.8
|
23.1
|
1.0
|
N
|
D:SER306
|
4.8
|
32.7
|
1.0
|
CA
|
D:SER306
|
5.0
|
28.6
|
1.0
|
|
Potassium binding site 3 out
of 9 in 7mtu
Go back to
Potassium Binding Sites List in 7mtu
Potassium binding site 3 out
of 9 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P221
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 P221 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K501
b:22.4
occ:1.00
|
O
|
A:GLY303
|
2.7
|
22.0
|
1.0
|
O
|
C:GLU470
|
2.7
|
20.7
|
1.0
|
O
|
A:CYS308
|
2.8
|
16.9
|
1.0
|
O
|
A:GLY305
|
2.8
|
21.9
|
1.0
|
O
|
C:SER471
|
2.8
|
26.4
|
1.0
|
O
|
C:HIS472
|
3.0
|
23.0
|
1.0
|
O
|
A:HOH641
|
3.1
|
18.1
|
1.0
|
C
|
C:SER471
|
3.3
|
21.6
|
1.0
|
C
|
C:HIS472
|
3.5
|
25.5
|
1.0
|
C
|
A:CYS308
|
3.7
|
18.3
|
1.0
|
CB
|
A:CYS308
|
3.8
|
19.8
|
1.0
|
C
|
C:GLU470
|
3.8
|
19.6
|
1.0
|
C
|
A:GLY305
|
3.9
|
26.5
|
1.0
|
C
|
A:GLY303
|
3.9
|
20.0
|
1.0
|
CA
|
C:SER471
|
3.9
|
22.2
|
1.0
|
C
|
A:PRO304
|
4.0
|
17.8
|
1.0
|
N
|
C:HIS472
|
4.0
|
18.0
|
1.0
|
CA
|
A:CYS308
|
4.1
|
21.4
|
1.0
|
N
|
A:GLY305
|
4.1
|
22.1
|
1.0
|
N
|
C:PRO473
|
4.2
|
27.0
|
1.0
|
N
|
A:CYS308
|
4.2
|
19.4
|
1.0
|
O
|
A:PRO304
|
4.2
|
21.0
|
1.0
|
CA
|
C:HIS472
|
4.2
|
28.2
|
1.0
|
CA
|
A:PRO304
|
4.3
|
21.4
|
1.0
|
SG
|
A:CYS308
|
4.3
|
23.5
|
1.0
|
N
|
C:SER471
|
4.4
|
23.2
|
1.0
|
CA
|
C:PRO473
|
4.5
|
24.4
|
1.0
|
CA
|
A:GLY305
|
4.6
|
23.9
|
1.0
|
CD2
|
C:HIS474
|
4.6
|
22.7
|
1.0
|
N
|
A:PRO304
|
4.6
|
23.8
|
1.0
|
N
|
A:THR309
|
4.7
|
19.2
|
1.0
|
NE2
|
C:HIS474
|
4.9
|
27.1
|
1.0
|
N
|
A:SER306
|
4.9
|
25.8
|
1.0
|
CA
|
A:GLY303
|
5.0
|
20.6
|
1.0
|
|
Potassium binding site 4 out
of 9 in 7mtu
Go back to
Potassium Binding Sites List in 7mtu
Potassium binding site 4 out
of 9 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P221
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 P221 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K501
b:23.3
occ:1.00
|
O
|
C:GLY305
|
2.8
|
25.8
|
1.0
|
O
|
D:GLU470
|
2.8
|
29.6
|
1.0
|
O
|
C:GLY303
|
2.8
|
26.5
|
1.0
|
O
|
D:SER471
|
2.8
|
23.3
|
1.0
|
O
|
C:CYS308
|
2.9
|
24.2
|
1.0
|
O
|
D:HIS472
|
3.0
|
26.1
|
1.0
|
C
|
D:SER471
|
3.3
|
25.6
|
1.0
|
O
|
C:HOH645
|
3.3
|
20.3
|
1.0
|
C
|
D:HIS472
|
3.5
|
29.1
|
1.0
|
C
|
C:CYS308
|
3.7
|
28.2
|
1.0
|
CB
|
C:CYS308
|
3.8
|
25.2
|
1.0
|
C
|
D:GLU470
|
3.9
|
26.9
|
1.0
|
N
|
D:HIS472
|
3.9
|
24.0
|
1.0
|
C
|
C:GLY305
|
3.9
|
24.7
|
1.0
|
CA
|
D:SER471
|
4.0
|
26.7
|
1.0
|
N
|
D:PRO473
|
4.0
|
27.3
|
1.0
|
C
|
C:GLY303
|
4.0
|
21.7
|
1.0
|
CA
|
C:CYS308
|
4.1
|
26.0
|
1.0
|
CA
|
D:HIS472
|
4.1
|
28.2
|
1.0
|
C
|
C:PRO304
|
4.1
|
25.2
|
1.0
|
N
|
C:CYS308
|
4.2
|
27.1
|
1.0
|
N
|
C:GLY305
|
4.3
|
25.3
|
1.0
|
O
|
C:PRO304
|
4.3
|
20.5
|
1.0
|
CD2
|
D:HIS474
|
4.3
|
24.6
|
1.0
|
SG
|
C:CYS308
|
4.3
|
34.6
|
1.0
|
CA
|
D:PRO473
|
4.4
|
26.7
|
1.0
|
N
|
D:SER471
|
4.4
|
26.0
|
1.0
|
CA
|
C:PRO304
|
4.5
|
22.6
|
1.0
|
NE2
|
D:HIS474
|
4.5
|
22.5
|
1.0
|
CA
|
C:GLY305
|
4.7
|
22.9
|
1.0
|
N
|
C:THR309
|
4.7
|
25.8
|
1.0
|
N
|
C:PRO304
|
4.8
|
20.4
|
1.0
|
CD
|
D:PRO473
|
4.8
|
30.2
|
1.0
|
N
|
C:SER306
|
4.9
|
28.2
|
1.0
|
|
Potassium binding site 5 out
of 9 in 7mtu
Go back to
Potassium Binding Sites List in 7mtu
Potassium binding site 5 out
of 9 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P221
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 P221 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K503
b:37.8
occ:1.00
|
O
|
F:GLY305
|
2.7
|
30.4
|
1.0
|
O
|
E:GLU470
|
2.7
|
30.8
|
1.0
|
O
|
E:SER471
|
2.8
|
40.3
|
1.0
|
O
|
F:GLY303
|
2.8
|
47.5
|
1.0
|
O
|
F:CYS308
|
2.9
|
30.1
|
1.0
|
O
|
E:HIS472
|
2.9
|
33.4
|
1.0
|
C
|
E:SER471
|
3.3
|
33.6
|
1.0
|
C
|
E:HIS472
|
3.4
|
34.2
|
1.0
|
C
|
F:CYS308
|
3.8
|
33.5
|
1.0
|
C
|
E:GLU470
|
3.8
|
30.0
|
1.0
|
C
|
F:GLY305
|
3.9
|
32.8
|
1.0
|
N
|
E:PRO473
|
3.9
|
30.5
|
1.0
|
N
|
E:HIS472
|
4.0
|
30.2
|
1.0
|
CA
|
E:SER471
|
4.0
|
30.8
|
1.0
|
CB
|
F:CYS308
|
4.0
|
27.6
|
1.0
|
C
|
F:GLY303
|
4.1
|
46.5
|
1.0
|
C
|
F:PRO304
|
4.1
|
30.9
|
1.0
|
CA
|
E:HIS472
|
4.1
|
35.5
|
1.0
|
N
|
F:GLY305
|
4.2
|
29.1
|
1.0
|
CA
|
E:PRO473
|
4.2
|
30.0
|
1.0
|
O
|
F:PRO304
|
4.2
|
35.2
|
1.0
|
CA
|
F:CYS308
|
4.2
|
31.4
|
1.0
|
N
|
F:CYS308
|
4.3
|
31.8
|
1.0
|
CD2
|
E:HIS474
|
4.3
|
33.5
|
1.0
|
N
|
E:SER471
|
4.4
|
33.3
|
1.0
|
CA
|
F:PRO304
|
4.4
|
39.5
|
1.0
|
SG
|
F:CYS308
|
4.4
|
37.6
|
1.0
|
CA
|
F:GLY305
|
4.6
|
35.0
|
1.0
|
NE2
|
E:HIS474
|
4.7
|
34.9
|
1.0
|
CD
|
E:PRO473
|
4.7
|
35.3
|
1.0
|
N
|
F:PRO304
|
4.8
|
40.2
|
1.0
|
N
|
F:THR309
|
4.8
|
34.0
|
1.0
|
N
|
F:SER306
|
4.9
|
35.6
|
1.0
|
C
|
F:SER306
|
5.0
|
30.5
|
1.0
|
|
Potassium binding site 6 out
of 9 in 7mtu
Go back to
Potassium Binding Sites List in 7mtu
Potassium binding site 6 out
of 9 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P221
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 P221 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K503
b:20.4
occ:1.00
|
O
|
F:SER471
|
2.7
|
25.3
|
1.0
|
O
|
H:GLY305
|
2.8
|
26.4
|
1.0
|
O
|
H:GLY303
|
2.8
|
26.7
|
1.0
|
O
|
F:GLU470
|
2.8
|
22.1
|
1.0
|
O
|
H:CYS308
|
2.9
|
23.8
|
1.0
|
O
|
H:HOH621
|
2.9
|
18.1
|
1.0
|
O
|
F:HIS472
|
3.2
|
27.7
|
1.0
|
C
|
F:SER471
|
3.3
|
24.4
|
1.0
|
C
|
F:HIS472
|
3.6
|
28.4
|
1.0
|
C
|
H:CYS308
|
3.7
|
20.3
|
1.0
|
CB
|
H:CYS308
|
3.8
|
26.4
|
1.0
|
C
|
H:GLY305
|
3.9
|
24.3
|
1.0
|
C
|
F:GLU470
|
3.9
|
24.8
|
1.0
|
CA
|
F:SER471
|
3.9
|
24.7
|
1.0
|
C
|
H:GLY303
|
4.0
|
27.7
|
1.0
|
C
|
H:PRO304
|
4.0
|
21.9
|
1.0
|
N
|
F:HIS472
|
4.0
|
23.5
|
1.0
|
CA
|
H:CYS308
|
4.1
|
21.3
|
1.0
|
N
|
F:PRO473
|
4.1
|
26.9
|
1.0
|
N
|
H:GLY305
|
4.1
|
22.3
|
1.0
|
N
|
H:CYS308
|
4.2
|
25.1
|
1.0
|
CA
|
F:HIS472
|
4.2
|
25.0
|
1.0
|
O
|
H:PRO304
|
4.3
|
24.4
|
1.0
|
SG
|
H:CYS308
|
4.3
|
29.0
|
1.0
|
CA
|
H:PRO304
|
4.4
|
28.1
|
1.0
|
N
|
F:SER471
|
4.4
|
23.7
|
1.0
|
CA
|
F:PRO473
|
4.5
|
27.9
|
1.0
|
CA
|
H:GLY305
|
4.6
|
23.8
|
1.0
|
CE1
|
F:HIS474
|
4.6
|
29.4
|
1.0
|
ND1
|
F:HIS474
|
4.6
|
29.5
|
1.0
|
N
|
H:THR309
|
4.7
|
18.6
|
1.0
|
N
|
H:PRO304
|
4.7
|
28.3
|
1.0
|
CD
|
F:PRO473
|
4.9
|
30.3
|
1.0
|
N
|
H:SER306
|
4.9
|
25.0
|
1.0
|
|
Potassium binding site 7 out
of 9 in 7mtu
Go back to
Potassium Binding Sites List in 7mtu
Potassium binding site 7 out
of 9 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P221
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 P221 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:K501
b:37.3
occ:1.00
|
O
|
E:GLY303
|
2.8
|
30.8
|
1.0
|
O
|
E:GLY305
|
2.8
|
35.1
|
1.0
|
O
|
G:GLU470
|
2.8
|
35.4
|
1.0
|
O
|
G:SER471
|
2.8
|
32.0
|
1.0
|
O
|
E:CYS308
|
2.8
|
28.4
|
1.0
|
O
|
G:HIS472
|
3.2
|
35.4
|
1.0
|
C
|
G:SER471
|
3.4
|
31.6
|
1.0
|
O
|
E:HOH610
|
3.4
|
25.6
|
1.0
|
C
|
E:CYS308
|
3.6
|
31.6
|
1.0
|
C
|
G:HIS472
|
3.7
|
35.5
|
1.0
|
CB
|
E:CYS308
|
3.7
|
33.2
|
1.0
|
C
|
G:GLU470
|
3.9
|
33.9
|
1.0
|
C
|
E:GLY305
|
3.9
|
34.5
|
1.0
|
C
|
E:GLY303
|
4.0
|
32.1
|
1.0
|
CA
|
G:SER471
|
4.0
|
32.0
|
1.0
|
CA
|
E:CYS308
|
4.0
|
32.2
|
1.0
|
N
|
G:HIS472
|
4.0
|
33.9
|
1.0
|
C
|
E:PRO304
|
4.1
|
36.2
|
1.0
|
N
|
E:CYS308
|
4.2
|
36.0
|
1.0
|
N
|
E:GLY305
|
4.2
|
37.6
|
1.0
|
N
|
G:PRO473
|
4.2
|
39.4
|
1.0
|
SG
|
E:CYS308
|
4.3
|
42.8
|
1.0
|
O
|
E:PRO304
|
4.3
|
27.9
|
1.0
|
CA
|
G:HIS472
|
4.3
|
32.8
|
1.0
|
CD2
|
G:HIS474
|
4.4
|
37.2
|
1.0
|
N
|
G:SER471
|
4.4
|
33.6
|
1.0
|
CA
|
E:PRO304
|
4.5
|
35.7
|
1.0
|
NE2
|
G:HIS474
|
4.5
|
32.7
|
1.0
|
CA
|
E:GLY305
|
4.6
|
34.3
|
1.0
|
CA
|
G:PRO473
|
4.6
|
37.5
|
1.0
|
N
|
E:THR309
|
4.7
|
31.6
|
1.0
|
N
|
E:PRO304
|
4.7
|
28.6
|
1.0
|
CA
|
E:GLY303
|
4.9
|
35.5
|
1.0
|
N
|
E:SER306
|
5.0
|
34.2
|
1.0
|
|
Potassium binding site 8 out
of 9 in 7mtu
Go back to
Potassium Binding Sites List in 7mtu
Potassium binding site 8 out
of 9 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P221
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 P221 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:K501
b:29.2
occ:1.00
|
O
|
H:GLU470
|
2.7
|
22.1
|
1.0
|
O
|
G:GLY305
|
2.8
|
20.0
|
1.0
|
O
|
G:GLY303
|
2.8
|
23.9
|
1.0
|
O
|
G:CYS308
|
2.8
|
28.0
|
1.0
|
O
|
H:SER471
|
2.8
|
25.6
|
1.0
|
O
|
H:HIS472
|
3.1
|
20.9
|
1.0
|
O
|
H:HOH636
|
3.2
|
19.8
|
1.0
|
C
|
H:SER471
|
3.4
|
22.1
|
1.0
|
C
|
G:CYS308
|
3.6
|
22.2
|
1.0
|
C
|
H:HIS472
|
3.6
|
24.8
|
1.0
|
CB
|
G:CYS308
|
3.7
|
22.7
|
1.0
|
C
|
G:GLY305
|
3.9
|
28.5
|
1.0
|
C
|
H:GLU470
|
3.9
|
23.5
|
1.0
|
C
|
G:PRO304
|
3.9
|
24.9
|
1.0
|
C
|
G:GLY303
|
3.9
|
24.8
|
1.0
|
CA
|
H:SER471
|
4.0
|
26.6
|
1.0
|
CA
|
G:CYS308
|
4.0
|
22.6
|
1.0
|
N
|
G:GLY305
|
4.0
|
20.3
|
1.0
|
O
|
G:PRO304
|
4.1
|
24.0
|
1.0
|
N
|
H:HIS472
|
4.1
|
21.0
|
1.0
|
N
|
G:CYS308
|
4.2
|
27.1
|
1.0
|
SG
|
G:CYS308
|
4.2
|
29.9
|
1.0
|
N
|
H:PRO473
|
4.2
|
32.7
|
1.0
|
CA
|
G:PRO304
|
4.3
|
27.7
|
1.0
|
CA
|
H:HIS472
|
4.4
|
25.5
|
1.0
|
N
|
H:SER471
|
4.4
|
26.1
|
1.0
|
CD2
|
H:HIS474
|
4.5
|
24.9
|
1.0
|
CA
|
H:PRO473
|
4.5
|
26.8
|
1.0
|
CA
|
G:GLY305
|
4.6
|
24.6
|
1.0
|
N
|
G:PRO304
|
4.6
|
25.3
|
1.0
|
N
|
G:THR309
|
4.7
|
22.7
|
1.0
|
NE2
|
H:HIS474
|
4.7
|
25.6
|
1.0
|
CA
|
G:GLY303
|
4.9
|
25.6
|
1.0
|
N
|
G:SER306
|
4.9
|
23.1
|
1.0
|
|
Potassium binding site 9 out
of 9 in 7mtu
Go back to
Potassium Binding Sites List in 7mtu
Potassium binding site 9 out
of 9 in the Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P221
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 9 of Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase From Bacillus Anthracis in the Complex with Imp and the Inhibitor P221 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:K505
b:58.7
occ:1.00
|
O
|
H:SER373
|
3.0
|
42.4
|
1.0
|
O
|
H:ALA371
|
3.1
|
38.2
|
1.0
|
O
|
H:GLY375
|
3.6
|
62.7
|
1.0
|
O
|
H:GLU372
|
3.9
|
37.9
|
1.0
|
C
|
H:SER373
|
4.0
|
39.5
|
1.0
|
C
|
H:GLU372
|
4.1
|
37.9
|
1.0
|
O
|
H:HOH649
|
4.2
|
46.4
|
1.0
|
C
|
H:ALA371
|
4.3
|
38.8
|
1.0
|
NZ
|
H:LYS386
|
4.4
|
38.4
|
1.0
|
CA
|
H:GLU372
|
4.4
|
39.1
|
1.0
|
CA
|
H:PRO374
|
4.5
|
41.5
|
1.0
|
N
|
H:SER373
|
4.6
|
38.9
|
1.0
|
N
|
H:GLY375
|
4.6
|
53.3
|
1.0
|
OD2
|
H:ASP58
|
4.6
|
54.1
|
1.0
|
C
|
H:GLY375
|
4.7
|
56.8
|
1.0
|
N
|
H:PRO374
|
4.7
|
40.1
|
1.0
|
C
|
H:PRO374
|
4.7
|
44.8
|
1.0
|
N
|
H:GLU372
|
4.9
|
39.3
|
1.0
|
OE1
|
H:GLU376
|
4.9
|
83.4
|
1.0
|
CA
|
H:SER373
|
4.9
|
39.5
|
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 P221 To Be Published.
Page generated: Mon Aug 12 19:27:11 2024
|