Potassium in PDB 9i0k: Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Compressed
Enzymatic activity of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Compressed
All present enzymatic activity of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Compressed:
1.1.1.205;
Potassium Binding Sites:
The binding sites of Potassium atom in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Compressed
(pdb code 9i0k). 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, Compressed, PDB code: 9i0k:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 9i0k
Go back to
Potassium Binding Sites List in 9i0k
Potassium binding site 1 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Compressed
 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, Compressed within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K603
b:60.3
occ:1.00
|
O
|
D:GLY322
|
2.7
|
27.8
|
1.0
|
O
|
A:SER496
|
2.8
|
56.1
|
1.0
|
O
|
A:GLU495
|
2.8
|
54.4
|
1.0
|
O
|
D:GLY320
|
3.0
|
29.7
|
1.0
|
O
|
A:HIS497
|
3.2
|
55.8
|
1.0
|
O
|
D:CYS325
|
3.2
|
26.7
|
1.0
|
O
|
D:HOH706
|
3.3
|
27.0
|
1.0
|
C
|
A:SER496
|
3.4
|
52.0
|
1.0
|
C
|
A:HIS497
|
3.6
|
57.2
|
1.0
|
C
|
D:GLY322
|
3.8
|
22.8
|
1.0
|
C
|
A:GLU495
|
3.9
|
51.8
|
1.0
|
C
|
D:PRO321
|
4.0
|
25.3
|
1.0
|
CB
|
D:CYS325
|
4.0
|
23.7
|
1.0
|
CA
|
A:SER496
|
4.0
|
51.9
|
1.0
|
C
|
D:CYS325
|
4.0
|
24.6
|
1.0
|
CE1
|
A:HIS499
|
4.1
|
52.2
|
1.0
|
O
|
D:PRO321
|
4.1
|
26.9
|
1.0
|
N
|
A:HIS497
|
4.1
|
54.6
|
1.0
|
N
|
D:GLY322
|
4.2
|
25.5
|
1.0
|
N
|
A:PRO498
|
4.2
|
59.1
|
1.0
|
ND1
|
A:HIS499
|
4.2
|
52.6
|
1.0
|
C
|
D:GLY320
|
4.2
|
27.4
|
1.0
|
N
|
D:CYS325
|
4.2
|
20.7
|
1.0
|
CA
|
D:CYS325
|
4.3
|
21.4
|
1.0
|
CA
|
A:HIS497
|
4.3
|
55.7
|
1.0
|
CA
|
D:PRO321
|
4.3
|
26.5
|
1.0
|
CA
|
A:PRO498
|
4.4
|
57.3
|
1.0
|
N
|
A:SER496
|
4.4
|
52.5
|
1.0
|
CA
|
D:GLY322
|
4.6
|
23.0
|
1.0
|
N
|
D:PRO321
|
4.8
|
28.7
|
1.0
|
N
|
D:SER323
|
4.8
|
19.7
|
1.0
|
CA
|
D:SER323
|
4.9
|
19.4
|
1.0
|
C
|
D:SER323
|
4.9
|
21.9
|
1.0
|
|
Potassium binding site 2 out
of 8 in 9i0k
Go back to
Potassium Binding Sites List in 9i0k
Potassium binding site 2 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Compressed
 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, Compressed within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K601
b:46.0
occ:1.00
|
O
|
A:GLY322
|
2.7
|
28.2
|
1.0
|
O
|
B:SER496
|
2.9
|
43.7
|
1.0
|
O
|
B:GLU495
|
2.9
|
43.8
|
1.0
|
O
|
B:HOH706
|
3.0
|
30.5
|
1.0
|
O
|
A:GLY320
|
3.1
|
28.7
|
1.0
|
O
|
B:HIS497
|
3.2
|
46.3
|
1.0
|
O
|
A:CYS325
|
3.2
|
25.1
|
1.0
|
C
|
B:SER496
|
3.4
|
40.7
|
1.0
|
C
|
B:HIS497
|
3.6
|
40.3
|
1.0
|
CB
|
A:CYS325
|
3.9
|
27.5
|
1.0
|
C
|
A:GLY322
|
3.9
|
23.6
|
1.0
|
C
|
A:CYS325
|
4.0
|
26.3
|
1.0
|
C
|
B:GLU495
|
4.0
|
40.5
|
1.0
|
CA
|
B:SER496
|
4.0
|
39.5
|
1.0
|
N
|
B:PRO498
|
4.0
|
40.6
|
1.0
|
N
|
B:HIS497
|
4.0
|
39.6
|
1.0
|
C
|
A:PRO321
|
4.1
|
24.4
|
1.0
|
O
|
A:PRO321
|
4.1
|
26.0
|
1.0
|
N
|
A:CYS325
|
4.2
|
24.1
|
1.0
|
C
|
A:GLY320
|
4.2
|
26.9
|
1.0
|
CA
|
B:HIS497
|
4.2
|
38.1
|
1.0
|
CA
|
A:CYS325
|
4.2
|
25.8
|
1.0
|
CE1
|
B:HIS499
|
4.2
|
36.4
|
1.0
|
N
|
A:GLY322
|
4.2
|
24.8
|
1.0
|
ND1
|
B:HIS499
|
4.3
|
37.3
|
1.0
|
CA
|
B:PRO498
|
4.3
|
38.2
|
1.0
|
N
|
B:SER496
|
4.5
|
38.4
|
1.0
|
CA
|
A:PRO321
|
4.5
|
25.6
|
1.0
|
CA
|
A:GLY322
|
4.7
|
22.3
|
1.0
|
CD
|
B:PRO498
|
4.9
|
38.1
|
1.0
|
N
|
A:PRO321
|
4.9
|
28.6
|
1.0
|
N
|
A:SER323
|
4.9
|
22.7
|
1.0
|
C
|
A:SER323
|
4.9
|
25.2
|
1.0
|
CA
|
A:SER323
|
4.9
|
22.9
|
1.0
|
|
Potassium binding site 3 out
of 8 in 9i0k
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Potassium Binding Sites List in 9i0k
Potassium binding site 3 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Compressed
 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, Compressed within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K601
b:41.7
occ:1.00
|
O
|
C:SER496
|
2.7
|
48.3
|
1.0
|
O
|
B:GLY322
|
2.8
|
27.3
|
1.0
|
O
|
C:GLU495
|
2.9
|
48.3
|
1.0
|
O
|
B:CYS325
|
3.0
|
25.8
|
1.0
|
O
|
B:GLY320
|
3.0
|
26.9
|
1.0
|
O
|
C:HIS497
|
3.1
|
46.2
|
1.0
|
C
|
C:SER496
|
3.3
|
42.8
|
1.0
|
C
|
C:HIS497
|
3.5
|
43.3
|
1.0
|
O
|
B:HOH703
|
3.7
|
30.0
|
1.0
|
C
|
B:CYS325
|
3.8
|
25.4
|
1.0
|
C
|
B:GLY322
|
3.9
|
22.5
|
1.0
|
CB
|
B:CYS325
|
3.9
|
24.9
|
1.0
|
C
|
C:GLU495
|
4.0
|
43.9
|
1.0
|
CA
|
C:SER496
|
4.0
|
41.6
|
1.0
|
N
|
C:HIS497
|
4.0
|
41.5
|
1.0
|
N
|
C:PRO498
|
4.1
|
42.9
|
1.0
|
N
|
B:CYS325
|
4.1
|
23.6
|
1.0
|
C
|
B:PRO321
|
4.1
|
24.1
|
1.0
|
CA
|
B:CYS325
|
4.2
|
24.9
|
1.0
|
CE1
|
C:HIS499
|
4.2
|
39.7
|
1.0
|
C
|
B:GLY320
|
4.2
|
26.5
|
1.0
|
ND1
|
C:HIS499
|
4.2
|
38.9
|
1.0
|
CA
|
C:HIS497
|
4.3
|
40.1
|
1.0
|
N
|
B:GLY322
|
4.3
|
25.2
|
1.0
|
O
|
B:PRO321
|
4.3
|
26.1
|
1.0
|
CA
|
C:PRO498
|
4.4
|
40.6
|
1.0
|
CA
|
B:PRO321
|
4.5
|
24.9
|
1.0
|
N
|
C:SER496
|
4.5
|
42.4
|
1.0
|
CA
|
B:GLY322
|
4.7
|
21.3
|
1.0
|
N
|
B:PRO321
|
4.9
|
28.8
|
1.0
|
N
|
B:SER323
|
4.9
|
20.6
|
1.0
|
C
|
B:SER323
|
4.9
|
23.4
|
1.0
|
CD
|
C:PRO498
|
4.9
|
40.5
|
1.0
|
CA
|
B:SER323
|
4.9
|
20.9
|
1.0
|
N
|
B:THR326
|
5.0
|
25.8
|
1.0
|
|
Potassium binding site 4 out
of 8 in 9i0k
Go back to
Potassium Binding Sites List in 9i0k
Potassium binding site 4 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Compressed
 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, Compressed within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K601
b:46.3
occ:1.00
|
O
|
C:GLY322
|
2.7
|
31.0
|
1.0
|
O
|
D:SER496
|
2.8
|
51.5
|
1.0
|
O
|
D:GLU495
|
2.9
|
48.8
|
1.0
|
O
|
C:GLY320
|
3.0
|
30.4
|
1.0
|
O
|
C:CYS325
|
3.0
|
30.0
|
1.0
|
O
|
C:HOH703
|
3.1
|
29.7
|
1.0
|
O
|
D:HIS497
|
3.2
|
48.2
|
1.0
|
C
|
D:SER496
|
3.4
|
45.6
|
1.0
|
C
|
D:HIS497
|
3.7
|
47.4
|
1.0
|
CB
|
C:CYS325
|
3.8
|
27.6
|
1.0
|
C
|
C:GLY322
|
3.9
|
25.4
|
1.0
|
C
|
C:CYS325
|
3.9
|
26.7
|
1.0
|
C
|
C:PRO321
|
4.0
|
25.3
|
1.0
|
C
|
D:GLU495
|
4.0
|
44.6
|
1.0
|
CA
|
D:SER496
|
4.1
|
45.1
|
1.0
|
N
|
C:CYS325
|
4.1
|
23.6
|
1.0
|
O
|
C:PRO321
|
4.1
|
25.0
|
1.0
|
CE1
|
D:HIS499
|
4.1
|
42.3
|
1.0
|
C
|
C:GLY320
|
4.1
|
30.2
|
1.0
|
CA
|
C:CYS325
|
4.1
|
25.0
|
1.0
|
N
|
D:HIS497
|
4.1
|
44.8
|
1.0
|
N
|
D:PRO498
|
4.2
|
46.8
|
1.0
|
ND1
|
D:HIS499
|
4.2
|
42.9
|
1.0
|
N
|
C:GLY322
|
4.2
|
27.3
|
1.0
|
CA
|
D:HIS497
|
4.4
|
46.9
|
1.0
|
CA
|
C:PRO321
|
4.4
|
28.5
|
1.0
|
CA
|
D:PRO498
|
4.5
|
42.7
|
1.0
|
N
|
D:SER496
|
4.5
|
44.4
|
1.0
|
CA
|
C:GLY322
|
4.7
|
23.9
|
1.0
|
N
|
C:PRO321
|
4.8
|
31.1
|
1.0
|
C
|
C:SER323
|
4.8
|
21.8
|
1.0
|
N
|
C:SER323
|
4.8
|
20.4
|
1.0
|
O
|
C:SER323
|
4.9
|
23.7
|
1.0
|
CA
|
C:SER323
|
4.9
|
20.8
|
1.0
|
|
Potassium binding site 5 out
of 8 in 9i0k
Go back to
Potassium Binding Sites List in 9i0k
Potassium binding site 5 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Compressed
 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, Compressed within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K603
b:39.9
occ:1.00
|
O
|
E:GLY322
|
2.6
|
26.4
|
1.0
|
O
|
E:GLY320
|
2.8
|
28.8
|
0.9
|
O
|
H:SER496
|
2.9
|
46.2
|
1.0
|
O
|
H:GLU495
|
3.0
|
46.3
|
1.0
|
O
|
E:CYS325
|
3.1
|
26.9
|
1.0
|
O
|
E:HOH709
|
3.2
|
28.0
|
1.0
|
O
|
H:HIS497
|
3.5
|
43.7
|
1.0
|
C
|
H:SER496
|
3.6
|
40.9
|
1.0
|
CB
|
E:CYS325
|
3.6
|
23.9
|
1.0
|
C
|
E:GLY322
|
3.8
|
21.9
|
1.0
|
C
|
E:CYS325
|
3.8
|
25.3
|
1.0
|
C
|
H:HIS497
|
3.9
|
39.8
|
1.0
|
C
|
E:PRO321
|
3.9
|
25.4
|
1.0
|
C
|
E:GLY320
|
3.9
|
29.4
|
0.9
|
N
|
E:GLY322
|
3.9
|
26.3
|
1.0
|
CA
|
E:CYS325
|
4.1
|
22.3
|
1.0
|
N
|
E:CYS325
|
4.1
|
21.9
|
1.0
|
C
|
H:GLU495
|
4.1
|
41.8
|
1.0
|
O
|
E:PRO321
|
4.2
|
26.5
|
1.0
|
CA
|
H:SER496
|
4.2
|
38.9
|
1.0
|
CA
|
E:PRO321
|
4.2
|
25.0
|
1.0
|
CE1
|
H:HIS499
|
4.2
|
38.6
|
1.0
|
N
|
H:PRO498
|
4.3
|
41.0
|
1.0
|
ND1
|
H:HIS499
|
4.3
|
40.0
|
1.0
|
N
|
H:HIS497
|
4.3
|
40.6
|
1.0
|
CA
|
E:GLY322
|
4.4
|
22.3
|
1.0
|
CA
|
H:PRO498
|
4.5
|
37.3
|
1.0
|
CA
|
H:HIS497
|
4.6
|
40.0
|
1.0
|
N
|
E:PRO321
|
4.6
|
28.4
|
1.0
|
N
|
H:SER496
|
4.6
|
39.7
|
1.0
|
N
|
E:SER323
|
4.8
|
19.1
|
1.0
|
N
|
E:THR326
|
4.9
|
24.5
|
1.0
|
C
|
E:SER323
|
5.0
|
21.2
|
1.0
|
CA
|
E:SER323
|
5.0
|
19.5
|
1.0
|
CA
|
E:GLY320
|
5.0
|
28.8
|
0.9
|
|
Potassium binding site 6 out
of 8 in 9i0k
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Potassium Binding Sites List in 9i0k
Potassium binding site 6 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Compressed
 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, Compressed within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K604
b:46.3
occ:1.00
|
O
|
F:GLY322
|
2.6
|
26.5
|
1.0
|
O
|
E:SER496
|
2.7
|
42.4
|
1.0
|
O
|
E:GLU495
|
2.7
|
43.7
|
1.0
|
O
|
F:GLY320
|
3.1
|
30.4
|
1.0
|
O
|
E:HIS497
|
3.1
|
40.6
|
1.0
|
O
|
F:CYS325
|
3.2
|
24.6
|
1.0
|
C
|
E:SER496
|
3.3
|
36.8
|
1.0
|
O
|
F:HOH708
|
3.6
|
58.5
|
1.0
|
C
|
E:HIS497
|
3.6
|
38.1
|
1.0
|
C
|
F:GLY322
|
3.8
|
22.7
|
1.0
|
C
|
E:GLU495
|
3.9
|
40.1
|
1.0
|
C
|
F:PRO321
|
4.0
|
25.0
|
1.0
|
CA
|
E:SER496
|
4.0
|
36.6
|
1.0
|
CD2
|
E:HIS499
|
4.1
|
35.9
|
1.0
|
N
|
E:HIS497
|
4.1
|
36.7
|
1.0
|
C
|
F:CYS325
|
4.1
|
24.6
|
1.0
|
O
|
F:PRO321
|
4.1
|
27.0
|
1.0
|
N
|
E:PRO498
|
4.1
|
39.2
|
1.0
|
CB
|
F:CYS325
|
4.1
|
24.4
|
1.0
|
N
|
F:GLY322
|
4.1
|
23.5
|
1.0
|
C
|
F:GLY320
|
4.2
|
28.5
|
1.0
|
N
|
F:CYS325
|
4.3
|
21.7
|
1.0
|
NE2
|
E:HIS499
|
4.3
|
35.8
|
1.0
|
CA
|
E:HIS497
|
4.3
|
37.3
|
1.0
|
CA
|
E:PRO498
|
4.3
|
39.5
|
1.0
|
CA
|
F:PRO321
|
4.4
|
24.9
|
1.0
|
N
|
E:SER496
|
4.4
|
38.1
|
1.0
|
CA
|
F:CYS325
|
4.4
|
22.4
|
1.0
|
CA
|
F:GLY322
|
4.6
|
20.6
|
1.0
|
N
|
F:SER323
|
4.7
|
21.5
|
1.0
|
N
|
F:PRO321
|
4.8
|
26.8
|
1.0
|
CA
|
F:SER323
|
4.8
|
20.3
|
1.0
|
C
|
F:SER323
|
4.8
|
24.1
|
1.0
|
O
|
F:SER323
|
4.9
|
25.9
|
1.0
|
|
Potassium binding site 7 out
of 8 in 9i0k
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Potassium Binding Sites List in 9i0k
Potassium binding site 7 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Compressed
 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, Compressed within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K603
b:50.9
occ:1.00
|
O
|
G:GLY322
|
2.8
|
26.3
|
1.0
|
O
|
G:GLY320
|
2.8
|
29.4
|
1.0
|
O
|
F:GLU495
|
2.8
|
48.2
|
1.0
|
O
|
F:SER496
|
2.9
|
44.7
|
1.0
|
O
|
G:CYS325
|
3.0
|
22.1
|
1.0
|
O
|
G:HOH709
|
3.1
|
44.6
|
1.0
|
O
|
F:HIS497
|
3.3
|
48.9
|
1.0
|
C
|
F:SER496
|
3.4
|
44.1
|
1.0
|
C
|
F:HIS497
|
3.8
|
45.5
|
1.0
|
C
|
G:CYS325
|
3.8
|
24.3
|
1.0
|
CB
|
G:CYS325
|
3.9
|
23.3
|
1.0
|
C
|
G:GLY322
|
3.9
|
20.5
|
1.0
|
C
|
G:PRO321
|
3.9
|
21.3
|
1.0
|
C
|
G:GLY320
|
3.9
|
25.2
|
1.0
|
C
|
F:GLU495
|
4.0
|
45.9
|
1.0
|
CA
|
F:SER496
|
4.0
|
45.0
|
1.0
|
N
|
G:GLY322
|
4.1
|
21.7
|
1.0
|
O
|
G:PRO321
|
4.1
|
23.8
|
1.0
|
N
|
F:HIS497
|
4.2
|
44.9
|
1.0
|
CA
|
G:CYS325
|
4.2
|
21.8
|
1.0
|
N
|
G:CYS325
|
4.2
|
19.9
|
1.0
|
CA
|
G:PRO321
|
4.3
|
22.9
|
1.0
|
N
|
F:PRO498
|
4.3
|
46.4
|
1.0
|
CA
|
F:HIS497
|
4.4
|
44.6
|
1.0
|
CD2
|
F:HIS499
|
4.4
|
44.2
|
1.0
|
N
|
F:SER496
|
4.5
|
45.4
|
1.0
|
CA
|
G:GLY322
|
4.6
|
19.4
|
1.0
|
N
|
G:PRO321
|
4.6
|
25.4
|
1.0
|
CA
|
F:PRO498
|
4.6
|
44.9
|
1.0
|
NE2
|
F:HIS499
|
4.7
|
43.5
|
1.0
|
CA
|
G:GLY320
|
4.9
|
25.9
|
1.0
|
N
|
G:THR326
|
4.9
|
23.1
|
1.0
|
N
|
G:SER323
|
4.9
|
18.9
|
1.0
|
|
Potassium binding site 8 out
of 8 in 9i0k
Go back to
Potassium Binding Sites List in 9i0k
Potassium binding site 8 out
of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) E- Xmp* Intermediate, Compressed
 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, Compressed within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:K603
b:58.0
occ:1.00
|
O
|
G:SER496
|
2.8
|
52.7
|
1.0
|
O
|
H:GLY322
|
2.8
|
26.8
|
1.0
|
O
|
G:GLU495
|
2.9
|
51.9
|
1.0
|
O
|
H:CYS325
|
3.1
|
26.7
|
1.0
|
O
|
G:HIS497
|
3.2
|
52.1
|
1.0
|
O
|
H:HOH708
|
3.3
|
30.2
|
1.0
|
O
|
H:GLY320
|
3.3
|
29.2
|
1.0
|
C
|
G:SER496
|
3.4
|
50.8
|
1.0
|
C
|
G:HIS497
|
3.6
|
53.0
|
1.0
|
C
|
H:CYS325
|
3.9
|
23.6
|
1.0
|
C
|
H:GLY322
|
3.9
|
22.0
|
1.0
|
N
|
G:PRO498
|
4.0
|
53.9
|
1.0
|
C
|
G:GLU495
|
4.0
|
51.4
|
1.0
|
CB
|
H:CYS325
|
4.0
|
23.6
|
1.0
|
CA
|
G:SER496
|
4.1
|
47.8
|
1.0
|
N
|
G:HIS497
|
4.2
|
50.6
|
1.0
|
N
|
H:CYS325
|
4.2
|
20.4
|
1.0
|
CE1
|
G:HIS499
|
4.2
|
53.3
|
1.0
|
CA
|
G:PRO498
|
4.2
|
53.7
|
1.0
|
CA
|
H:CYS325
|
4.3
|
22.6
|
1.0
|
ND1
|
G:HIS499
|
4.3
|
54.8
|
1.0
|
C
|
H:PRO321
|
4.3
|
24.5
|
1.0
|
CA
|
G:HIS497
|
4.3
|
51.6
|
1.0
|
N
|
H:GLY322
|
4.4
|
25.8
|
1.0
|
O
|
H:PRO321
|
4.4
|
27.3
|
1.0
|
C
|
H:GLY320
|
4.4
|
26.5
|
1.0
|
N
|
G:SER496
|
4.5
|
49.8
|
1.0
|
CA
|
H:PRO321
|
4.7
|
25.1
|
1.0
|
CA
|
H:GLY322
|
4.8
|
22.0
|
1.0
|
C
|
H:SER323
|
4.9
|
22.3
|
1.0
|
CD
|
G:PRO498
|
4.9
|
50.5
|
1.0
|
N
|
H:SER323
|
4.9
|
20.4
|
1.0
|
O
|
H:SER323
|
4.9
|
26.5
|
1.0
|
CA
|
H:SER323
|
4.9
|
20.0
|
1.0
|
N
|
H:THR326
|
5.0
|
22.3
|
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 19:11:42 2025
|