Potassium in PDB 9i0l: Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended
Enzymatic activity of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended
All present enzymatic activity of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended:
1.1.1.205;
Potassium Binding Sites:
The binding sites of Potassium atom in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended
(pdb code 9i0l). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 8 binding sites of Potassium where determined in the
Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended, PDB code: 9i0l:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 9i0l
Go back to
Potassium Binding Sites List in 9i0l
Potassium binding site 1 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K603
b:34.9
occ:1.00
|
O
|
D:GLY322
|
2.7
|
35.4
|
1.0
|
O
|
A:GLU495
|
2.9
|
33.7
|
1.0
|
O
|
D:GLY320
|
2.9
|
33.3
|
1.0
|
O
|
A:SER496
|
3.0
|
40.5
|
1.0
|
O
|
D:CYS325
|
3.2
|
39.0
|
1.0
|
O
|
A:HIS497
|
3.3
|
41.5
|
1.0
|
C
|
A:SER496
|
3.5
|
36.2
|
1.0
|
C
|
A:HIS497
|
3.6
|
36.9
|
1.0
|
C
|
D:GLY322
|
3.8
|
29.5
|
1.0
|
C
|
D:CYS325
|
3.9
|
34.1
|
1.0
|
CB
|
D:CYS325
|
4.0
|
28.3
|
1.0
|
C
|
A:GLU495
|
4.0
|
33.3
|
1.0
|
N
|
A:PRO498
|
4.1
|
37.9
|
1.0
|
C
|
D:PRO321
|
4.1
|
34.1
|
1.0
|
CA
|
A:SER496
|
4.1
|
34.3
|
1.0
|
N
|
A:HIS497
|
4.1
|
33.1
|
1.0
|
C
|
D:GLY320
|
4.2
|
28.9
|
1.0
|
N
|
D:GLY322
|
4.2
|
30.4
|
1.0
|
N
|
D:CYS325
|
4.2
|
33.2
|
1.0
|
CA
|
D:CYS325
|
4.3
|
30.7
|
1.0
|
ND1
|
A:HIS499
|
4.3
|
31.0
|
1.0
|
CA
|
A:HIS497
|
4.3
|
30.7
|
1.0
|
CA
|
A:PRO498
|
4.3
|
35.7
|
1.0
|
CE1
|
A:HIS499
|
4.4
|
30.0
|
1.0
|
O
|
D:PRO321
|
4.4
|
38.0
|
1.0
|
CA
|
D:PRO321
|
4.5
|
30.7
|
1.0
|
N
|
A:SER496
|
4.5
|
36.2
|
1.0
|
CA
|
D:GLY322
|
4.6
|
28.2
|
1.0
|
N
|
D:SER323
|
4.8
|
30.5
|
1.0
|
N
|
D:PRO321
|
4.8
|
29.1
|
1.0
|
C
|
D:SER323
|
4.9
|
33.6
|
1.0
|
CA
|
D:SER323
|
4.9
|
31.4
|
1.0
|
CD
|
A:PRO498
|
4.9
|
35.5
|
1.0
|
N
|
D:THR326
|
5.0
|
31.9
|
1.0
|
|
Potassium binding site 2 out
of 8 in 9i0l
Go back to
Potassium Binding Sites List in 9i0l
Potassium binding site 2 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K601
b:44.6
occ:1.00
|
O
|
A:GLY322
|
2.7
|
44.4
|
1.0
|
O
|
B:GLU495
|
2.7
|
42.2
|
1.0
|
O
|
A:GLY320
|
2.8
|
42.9
|
1.0
|
O
|
B:SER496
|
2.8
|
48.5
|
1.0
|
C
|
B:SER496
|
3.4
|
42.6
|
1.0
|
O
|
B:HIS497
|
3.4
|
48.3
|
1.0
|
O
|
A:CYS325
|
3.5
|
47.9
|
1.0
|
C
|
B:HIS497
|
3.8
|
49.3
|
1.0
|
C
|
A:GLY322
|
3.8
|
36.6
|
1.0
|
C
|
B:GLU495
|
3.9
|
39.9
|
1.0
|
C
|
A:PRO321
|
3.9
|
38.5
|
1.0
|
O
|
A:PRO321
|
4.0
|
42.1
|
1.0
|
C
|
A:GLY320
|
4.0
|
39.4
|
1.0
|
CA
|
B:SER496
|
4.0
|
41.1
|
1.0
|
CB
|
A:CYS325
|
4.1
|
38.9
|
1.0
|
N
|
B:HIS497
|
4.1
|
42.2
|
1.0
|
C
|
A:CYS325
|
4.2
|
43.0
|
1.0
|
N
|
A:GLY322
|
4.2
|
38.8
|
1.0
|
N
|
B:PRO498
|
4.3
|
48.7
|
1.0
|
CD2
|
B:HIS499
|
4.3
|
41.4
|
1.0
|
N
|
A:CYS325
|
4.4
|
40.9
|
1.0
|
CA
|
A:PRO321
|
4.4
|
36.6
|
1.0
|
CA
|
A:CYS325
|
4.4
|
38.6
|
1.0
|
CA
|
B:HIS497
|
4.4
|
47.3
|
1.0
|
N
|
B:SER496
|
4.4
|
42.1
|
1.0
|
NE2
|
B:HIS499
|
4.5
|
38.9
|
1.0
|
CA
|
B:PRO498
|
4.5
|
47.1
|
1.0
|
CA
|
A:GLY322
|
4.6
|
35.4
|
1.0
|
N
|
A:PRO321
|
4.7
|
36.5
|
1.0
|
N
|
A:SER323
|
4.8
|
34.2
|
1.0
|
CA
|
A:SER323
|
4.9
|
33.6
|
1.0
|
C
|
A:SER323
|
4.9
|
38.4
|
1.0
|
|
Potassium binding site 3 out
of 8 in 9i0l
Go back to
Potassium Binding Sites List in 9i0l
Potassium binding site 3 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K601
b:45.1
occ:1.00
|
O
|
B:GLY322
|
2.7
|
42.0
|
1.0
|
O
|
C:SER496
|
2.8
|
46.8
|
1.0
|
O
|
C:GLU495
|
2.9
|
44.4
|
1.0
|
O
|
B:GLY320
|
2.9
|
41.3
|
0.9
|
O
|
B:CYS325
|
3.1
|
39.1
|
1.0
|
O
|
C:HIS497
|
3.1
|
45.1
|
1.0
|
C
|
C:SER496
|
3.4
|
42.8
|
1.0
|
C
|
C:HIS497
|
3.6
|
43.5
|
1.0
|
C
|
B:GLY322
|
3.9
|
37.3
|
1.0
|
C
|
B:CYS325
|
4.0
|
39.1
|
1.0
|
C
|
C:GLU495
|
4.0
|
41.6
|
1.0
|
C
|
B:PRO321
|
4.0
|
43.0
|
1.0
|
N
|
C:PRO498
|
4.0
|
45.1
|
1.0
|
CB
|
B:CYS325
|
4.0
|
37.2
|
1.0
|
N
|
C:HIS497
|
4.1
|
35.7
|
1.0
|
C
|
B:GLY320
|
4.1
|
37.1
|
0.9
|
CA
|
C:SER496
|
4.1
|
41.8
|
1.0
|
O
|
B:PRO321
|
4.2
|
48.2
|
1.0
|
N
|
B:GLY322
|
4.2
|
38.5
|
1.0
|
CA
|
C:HIS497
|
4.3
|
36.1
|
1.0
|
N
|
B:CYS325
|
4.3
|
40.1
|
1.0
|
CA
|
C:PRO498
|
4.3
|
42.5
|
1.0
|
CA
|
B:CYS325
|
4.3
|
37.5
|
1.0
|
CD2
|
C:HIS499
|
4.3
|
40.0
|
1.0
|
CA
|
B:PRO321
|
4.4
|
37.6
|
1.0
|
NE2
|
C:HIS499
|
4.5
|
39.6
|
1.0
|
N
|
C:SER496
|
4.5
|
43.2
|
1.0
|
CA
|
B:GLY322
|
4.6
|
33.9
|
1.0
|
N
|
B:PRO321
|
4.7
|
35.8
|
1.0
|
N
|
B:SER323
|
4.8
|
35.9
|
1.0
|
CD
|
C:PRO498
|
4.9
|
41.1
|
1.0
|
CA
|
B:SER323
|
4.9
|
36.7
|
1.0
|
C
|
B:SER323
|
5.0
|
39.1
|
1.0
|
|
Potassium binding site 4 out
of 8 in 9i0l
Go back to
Potassium Binding Sites List in 9i0l
Potassium binding site 4 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K604
b:35.9
occ:1.00
|
O
|
C:GLY322
|
2.7
|
34.6
|
1.0
|
O
|
D:GLU495
|
2.8
|
35.2
|
1.0
|
O
|
C:GLY320
|
3.0
|
34.2
|
1.0
|
O
|
D:SER496
|
3.1
|
36.7
|
1.0
|
O
|
C:CYS325
|
3.3
|
32.5
|
1.0
|
O
|
D:HIS497
|
3.4
|
41.4
|
1.0
|
C
|
D:SER496
|
3.6
|
32.2
|
1.0
|
CB
|
C:CYS325
|
3.8
|
31.6
|
1.0
|
C
|
C:GLY322
|
3.8
|
27.2
|
1.0
|
C
|
C:PRO321
|
3.9
|
31.7
|
1.0
|
C
|
D:HIS497
|
3.9
|
35.2
|
1.0
|
C
|
C:CYS325
|
4.0
|
33.2
|
1.0
|
C
|
D:GLU495
|
4.0
|
33.3
|
1.0
|
C
|
C:GLY320
|
4.0
|
30.7
|
1.0
|
N
|
C:GLY322
|
4.0
|
27.7
|
1.0
|
O
|
C:PRO321
|
4.1
|
34.6
|
1.0
|
N
|
C:CYS325
|
4.2
|
28.8
|
1.0
|
CA
|
C:CYS325
|
4.2
|
30.6
|
1.0
|
CA
|
D:SER496
|
4.2
|
29.7
|
1.0
|
CA
|
C:PRO321
|
4.2
|
28.7
|
1.0
|
CD2
|
D:HIS499
|
4.3
|
34.1
|
1.0
|
N
|
D:HIS497
|
4.3
|
28.5
|
1.0
|
N
|
D:PRO498
|
4.4
|
36.5
|
1.0
|
NE2
|
D:HIS499
|
4.5
|
34.5
|
1.0
|
CA
|
C:GLY322
|
4.5
|
24.7
|
1.0
|
CA
|
D:HIS497
|
4.5
|
27.7
|
1.0
|
N
|
D:SER496
|
4.6
|
31.3
|
1.0
|
N
|
C:PRO321
|
4.6
|
27.7
|
1.0
|
CA
|
D:PRO498
|
4.7
|
29.3
|
1.0
|
N
|
C:SER323
|
4.8
|
28.0
|
1.0
|
CA
|
C:SER323
|
5.0
|
27.0
|
1.0
|
|
Potassium binding site 5 out
of 8 in 9i0l
Go back to
Potassium Binding Sites List in 9i0l
Potassium binding site 5 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K603
b:36.7
occ:1.00
|
O
|
E:GLY322
|
2.6
|
40.0
|
1.0
|
O
|
E:GLY320
|
2.8
|
35.5
|
1.0
|
O
|
H:SER496
|
2.9
|
46.4
|
1.0
|
O
|
E:CYS325
|
3.0
|
41.0
|
1.0
|
O
|
H:GLU495
|
3.1
|
42.0
|
1.0
|
O
|
H:HIS497
|
3.5
|
48.7
|
1.0
|
C
|
H:SER496
|
3.6
|
40.6
|
1.0
|
C
|
E:GLY322
|
3.8
|
32.2
|
1.0
|
CB
|
E:CYS325
|
3.8
|
31.2
|
1.0
|
C
|
E:CYS325
|
3.8
|
37.5
|
1.0
|
C
|
H:HIS497
|
3.8
|
44.6
|
1.0
|
C
|
E:PRO321
|
4.0
|
33.2
|
1.0
|
C
|
E:GLY320
|
4.0
|
31.1
|
1.0
|
N
|
E:CYS325
|
4.1
|
36.0
|
1.0
|
CA
|
E:CYS325
|
4.1
|
32.9
|
1.0
|
N
|
E:GLY322
|
4.1
|
32.6
|
1.0
|
O
|
E:PRO321
|
4.1
|
36.0
|
1.0
|
C
|
H:GLU495
|
4.2
|
39.6
|
1.0
|
CA
|
H:SER496
|
4.2
|
39.4
|
1.0
|
N
|
H:PRO498
|
4.2
|
45.3
|
1.0
|
N
|
H:HIS497
|
4.3
|
37.3
|
1.0
|
CA
|
E:PRO321
|
4.4
|
32.7
|
1.0
|
CD2
|
H:HIS499
|
4.4
|
39.4
|
1.0
|
NE2
|
H:HIS499
|
4.5
|
39.8
|
1.0
|
CA
|
H:PRO498
|
4.5
|
41.6
|
1.0
|
CA
|
H:HIS497
|
4.5
|
39.0
|
1.0
|
CA
|
E:GLY322
|
4.5
|
29.6
|
1.0
|
N
|
E:PRO321
|
4.7
|
31.2
|
1.0
|
N
|
H:SER496
|
4.7
|
41.0
|
1.0
|
N
|
E:SER323
|
4.7
|
33.7
|
1.0
|
CA
|
E:SER323
|
4.8
|
33.1
|
1.0
|
C
|
E:SER323
|
4.9
|
35.5
|
1.0
|
N
|
E:THR326
|
4.9
|
34.1
|
1.0
|
|
Potassium binding site 6 out
of 8 in 9i0l
Go back to
Potassium Binding Sites List in 9i0l
Potassium binding site 6 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K604
b:42.0
occ:1.00
|
O
|
F:GLY322
|
2.6
|
39.2
|
1.0
|
O
|
E:SER496
|
2.8
|
47.8
|
1.0
|
O
|
E:GLU495
|
3.0
|
41.9
|
1.0
|
O
|
F:CYS325
|
3.1
|
41.1
|
1.0
|
O
|
E:HIS497
|
3.2
|
45.1
|
1.0
|
O
|
F:GLY320
|
3.3
|
43.8
|
1.0
|
C
|
E:SER496
|
3.5
|
40.2
|
1.0
|
C
|
E:HIS497
|
3.6
|
44.8
|
1.0
|
C
|
F:GLY322
|
3.8
|
36.2
|
1.0
|
C
|
F:CYS325
|
3.9
|
38.9
|
1.0
|
CB
|
F:CYS325
|
3.9
|
35.4
|
1.0
|
N
|
E:PRO498
|
4.0
|
46.9
|
1.0
|
C
|
F:PRO321
|
4.1
|
37.9
|
1.0
|
C
|
E:GLU495
|
4.1
|
40.8
|
1.0
|
N
|
F:CYS325
|
4.1
|
35.6
|
1.0
|
N
|
F:GLY322
|
4.1
|
35.4
|
1.0
|
CD2
|
E:HIS499
|
4.2
|
39.9
|
1.0
|
CA
|
E:SER496
|
4.2
|
39.7
|
1.0
|
CA
|
F:CYS325
|
4.2
|
35.5
|
1.0
|
N
|
E:HIS497
|
4.2
|
38.2
|
1.0
|
CA
|
E:PRO498
|
4.2
|
42.9
|
1.0
|
O
|
F:PRO321
|
4.3
|
42.9
|
1.0
|
C
|
F:GLY320
|
4.4
|
39.6
|
1.0
|
CA
|
E:HIS497
|
4.4
|
37.9
|
1.0
|
NE2
|
E:HIS499
|
4.5
|
39.8
|
1.0
|
CA
|
F:PRO321
|
4.5
|
35.6
|
1.0
|
CA
|
F:GLY322
|
4.5
|
31.8
|
1.0
|
N
|
E:SER496
|
4.6
|
42.6
|
1.0
|
N
|
F:SER323
|
4.8
|
39.9
|
1.0
|
CD
|
E:PRO498
|
4.8
|
41.7
|
1.0
|
C
|
F:SER323
|
4.9
|
38.9
|
1.0
|
CA
|
F:SER323
|
4.9
|
36.6
|
1.0
|
N
|
F:PRO321
|
4.9
|
33.7
|
1.0
|
N
|
F:THR326
|
5.0
|
34.9
|
1.0
|
|
Potassium binding site 7 out
of 8 in 9i0l
Go back to
Potassium Binding Sites List in 9i0l
Potassium binding site 7 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 7 of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K603
b:37.9
occ:1.00
|
O
|
G:GLY322
|
2.7
|
36.2
|
1.0
|
O
|
F:SER496
|
2.7
|
42.9
|
1.0
|
O
|
G:GLY320
|
2.9
|
32.4
|
1.0
|
O
|
F:GLU495
|
3.0
|
35.9
|
1.0
|
O
|
G:CYS325
|
3.1
|
39.6
|
1.0
|
O
|
F:HIS497
|
3.4
|
46.0
|
1.0
|
C
|
F:SER496
|
3.5
|
35.8
|
1.0
|
C
|
F:HIS497
|
3.7
|
42.4
|
1.0
|
C
|
G:GLY322
|
3.8
|
31.1
|
1.0
|
C
|
G:CYS325
|
3.9
|
31.9
|
1.0
|
CB
|
G:CYS325
|
3.9
|
28.4
|
1.0
|
C
|
G:GLY320
|
4.1
|
28.7
|
1.0
|
C
|
G:PRO321
|
4.1
|
31.2
|
1.0
|
N
|
G:CYS325
|
4.1
|
32.3
|
1.0
|
N
|
F:PRO498
|
4.1
|
41.6
|
1.0
|
C
|
F:GLU495
|
4.1
|
33.1
|
1.0
|
N
|
G:GLY322
|
4.2
|
28.3
|
1.0
|
CA
|
G:CYS325
|
4.2
|
29.6
|
1.0
|
CA
|
F:SER496
|
4.2
|
31.2
|
1.0
|
N
|
F:HIS497
|
4.3
|
34.2
|
1.0
|
CD2
|
F:HIS499
|
4.4
|
35.2
|
1.0
|
O
|
G:PRO321
|
4.4
|
34.5
|
1.0
|
CA
|
F:PRO498
|
4.4
|
38.7
|
1.0
|
NE2
|
F:HIS499
|
4.4
|
31.5
|
1.0
|
CA
|
F:HIS497
|
4.4
|
36.8
|
1.0
|
CA
|
G:PRO321
|
4.5
|
29.1
|
1.0
|
CA
|
G:GLY322
|
4.6
|
25.5
|
1.0
|
N
|
F:SER496
|
4.7
|
34.4
|
1.0
|
N
|
G:PRO321
|
4.8
|
29.1
|
1.0
|
CD
|
F:PRO498
|
4.9
|
38.5
|
1.0
|
N
|
G:SER323
|
4.9
|
29.3
|
1.0
|
N
|
G:THR326
|
4.9
|
27.0
|
1.0
|
C
|
G:SER323
|
4.9
|
29.8
|
1.0
|
CA
|
G:SER323
|
5.0
|
28.7
|
1.0
|
|
Potassium binding site 8 out
of 8 in 9i0l
Go back to
Potassium Binding Sites List in 9i0l
Potassium binding site 8 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 8 of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Extended within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:K603
b:32.6
occ:1.00
|
O
|
H:GLY322
|
2.7
|
26.0
|
1.0
|
O
|
H:GLY320
|
2.8
|
31.2
|
1.0
|
O
|
G:GLU495
|
2.9
|
31.6
|
1.0
|
O
|
G:SER496
|
3.1
|
35.7
|
1.0
|
O
|
G:HIS497
|
3.1
|
35.5
|
1.0
|
O
|
H:CYS325
|
3.3
|
30.2
|
0.9
|
C
|
G:SER496
|
3.5
|
32.2
|
1.0
|
C
|
G:HIS497
|
3.6
|
30.1
|
1.0
|
CB
|
H:CYS325
|
3.8
|
26.0
|
0.9
|
C
|
H:GLY322
|
3.9
|
23.3
|
1.0
|
C
|
H:CYS325
|
3.9
|
26.2
|
0.9
|
C
|
H:GLY320
|
4.0
|
26.6
|
1.0
|
C
|
G:GLU495
|
4.0
|
27.4
|
1.0
|
C
|
H:PRO321
|
4.0
|
27.7
|
1.0
|
N
|
G:HIS497
|
4.1
|
31.1
|
1.0
|
CA
|
G:SER496
|
4.1
|
27.6
|
1.0
|
N
|
H:GLY322
|
4.2
|
23.0
|
1.0
|
N
|
G:PRO498
|
4.2
|
30.3
|
1.0
|
CA
|
H:CYS325
|
4.2
|
24.2
|
0.9
|
N
|
H:CYS325
|
4.2
|
21.6
|
0.9
|
O
|
H:PRO321
|
4.3
|
29.9
|
1.0
|
CD2
|
G:HIS499
|
4.3
|
26.5
|
1.0
|
CA
|
G:HIS497
|
4.3
|
28.3
|
1.0
|
CA
|
H:PRO321
|
4.4
|
25.0
|
1.0
|
NE2
|
G:HIS499
|
4.5
|
27.8
|
1.0
|
CA
|
G:PRO498
|
4.5
|
28.5
|
1.0
|
N
|
G:SER496
|
4.6
|
28.9
|
1.0
|
CA
|
H:GLY322
|
4.6
|
22.5
|
1.0
|
N
|
H:PRO321
|
4.7
|
23.3
|
1.0
|
N
|
H:SER323
|
4.9
|
23.2
|
1.0
|
CD
|
G:PRO498
|
5.0
|
28.2
|
1.0
|
N
|
H:THR326
|
5.0
|
22.2
|
1.0
|
|
Reference:
O.Bulvas,
Z.Knejzlik,
A.Filimonenko,
T.Kouba,
I.Pichova.
Conformational Landscape of the Mycobacterial Inosine 5'-Monophosphate Dehydrogenase Octamerization Interface. J.Struct.Biol. V. 217 08198 2025.
ISSN: ESSN 1095-8657
PubMed: 40107326
DOI: 10.1016/J.JSB.2025.108198
Page generated: Sat Aug 9 19:11:47 2025
|