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Potassium in PDB 9i0m: Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) Saturating Atp+Imp-Bound Form, Extended

Enzymatic activity of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) Saturating Atp+Imp-Bound Form, Extended

All present enzymatic activity of Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) Saturating Atp+Imp-Bound Form, Extended:
1.1.1.205;

Potassium Binding Sites:

The binding sites of Potassium atom in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) Saturating Atp+Imp-Bound Form, Extended (pdb code 9i0m). 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) Saturating Atp+Imp-Bound Form, Extended, PDB code: 9i0m:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Potassium binding site 1 out of 8 in 9i0m

Go back to Potassium Binding Sites List in 9i0m
Potassium binding site 1 out of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) Saturating Atp+Imp-Bound Form, 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) Saturating Atp+Imp-Bound Form, Extended within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K601

b:87.1
occ:1.00
 O A:CYS325 2.7 60.0 1.0
O B:SER496 2.8 82.5 1.0
O A:GLY322 2.8 54.1 1.0
O A:GLY320 3.1 51.8 1.0
O B:GLU495 3.2 81.2 1.0
O B:HIS497 3.4 92.7 1.0
C B:SER496 3.5 81.8 1.0
C A:CYS325 3.6 55.9 1.0
C B:HIS497 3.7 92.7 1.0
CB A:CYS325 3.9 49.9 1.0
C A:GLY322 4.0 49.4 1.0
N B:PRO498 4.1 94.0 1.0
CA A:CYS325 4.1 49.8 1.0
CA B:SER496 4.2 78.4 1.0
N B:HIS497 4.2 82.7 1.0
N A:CYS325 4.2 52.3 1.0
C A:GLY320 4.3 49.0 1.0
C B:GLU495 4.3 78.3 1.0
C A:PRO321 4.3 46.0 1.0
CA B:HIS497 4.3 89.1 1.0
CA B:PRO498 4.4 95.0 1.0
N A:GLY322 4.4 48.9 1.0
SG A:CYS325 4.6 65.8 1.0
CD2 B:HIS499 4.6 94.4 1.0
CA A:PRO321 4.6 43.4 1.0
O A:PRO321 4.6 45.7 1.0
N A:THR326 4.7 52.2 1.0
CD B:PRO498 4.7 91.4 1.0
CA A:GLY322 4.8 43.8 1.0
N B:SER496 4.8 78.1 1.0
O A:SER323 4.8 54.7 1.0
NE2 B:HIS499 4.8 92.7 1.0
CD A:ARG328 4.9 50.0 1.0
C A:SER323 4.9 53.7 1.0
N A:SER323 5.0 50.0 1.0
N A:PRO321 5.0 46.3 1.0

Potassium binding site 2 out of 8 in 9i0m

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Potassium binding site 2 out of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) Saturating Atp+Imp-Bound Form, 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) Saturating Atp+Imp-Bound Form, Extended within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K603

b:75.0
occ:1.00
 O B:GLY320 2.7 54.4 1.0
O B:GLY322 2.7 53.9 1.0
O D:SER496 2.9 95.7 1.0
O D:GLU495 3.0 95.5 1.0
O B:CYS325 3.3 61.9 1.0
C D:SER496 3.6 95.2 1.0
O D:HIS497 3.7 110.9 1.0
C B:GLY322 3.8 49.5 1.0
C B:GLY320 3.9 48.2 1.0
C B:PRO321 3.9 43.0 1.0
N B:GLY322 4.0 44.8 1.0
C B:CYS325 4.1 55.8 1.0
CA D:SER496 4.1 90.5 1.0
CB B:CYS325 4.1 49.4 1.0
C D:HIS497 4.1 109.5 1.0
CA B:PRO321 4.1 43.4 1.0
C D:GLU495 4.2 92.2 1.0
O B:PRO321 4.2 46.6 1.0
CD2 D:HIS499 4.5 107.5 1.0
CA B:CYS325 4.5 51.6 1.0
N D:HIS497 4.5 97.8 1.0
N B:PRO321 4.5 45.1 1.0
CA B:GLY322 4.5 46.0 1.0
N B:CYS325 4.6 52.3 1.0
NE2 D:HIS499 4.6 102.7 1.0
N D:PRO498 4.6 113.4 1.0
N D:SER496 4.6 92.0 1.0
SG B:CYS325 4.8 59.6 1.0
CA D:HIS497 4.8 103.6 1.0
CD B:ARG328 4.8 52.0 1.0
CA D:PRO498 4.8 114.8 1.0
N B:SER323 4.9 46.4 1.0
CA B:GLY320 5.0 45.2 1.0

Potassium binding site 3 out of 8 in 9i0m

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Potassium binding site 3 out of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) Saturating Atp+Imp-Bound Form, 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) Saturating Atp+Imp-Bound Form, Extended within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K602

b:116.1
occ:1.00
 O A:SER496 2.7 120.3 1.0
O C:CYS325 2.7 58.1 1.0
O C:GLY322 2.9 55.1 1.0
O C:GLY320 3.1 48.4 1.0
O A:GLU495 3.5 114.1 1.0
C A:SER496 3.6 116.7 1.0
O A:HIS497 3.6 127.2 1.0
C C:CYS325 3.6 53.1 1.0
C A:HIS497 3.8 127.7 1.0
CB C:CYS325 4.0 50.8 1.0
N A:PRO498 4.1 130.1 1.0
C C:GLY322 4.1 53.1 1.0
CA C:CYS325 4.1 53.0 1.0
N C:CYS325 4.2 50.0 1.0
N A:HIS497 4.3 115.2 1.0
C C:GLY320 4.4 46.0 1.0
CA A:SER496 4.4 110.4 1.0
CA A:PRO498 4.4 127.9 1.0
CA A:HIS497 4.4 120.9 1.0
C C:PRO321 4.6 46.1 1.0
N C:THR326 4.6 45.1 1.0
C A:GLU495 4.6 111.8 1.0
N C:GLY322 4.6 48.4 1.0
CD A:PRO498 4.7 124.1 1.0
SG C:CYS325 4.8 60.0 1.0
CA C:PRO321 4.8 40.7 1.0
O C:PRO321 4.8 47.5 1.0
CD2 A:HIS499 4.9 125.6 1.0
CA C:THR326 4.9 41.9 1.0
C C:SER323 4.9 56.7 1.0
CA C:GLY322 4.9 46.8 1.0
CA C:SER323 5.0 52.2 1.0
N A:SER496 5.0 111.6 1.0
CD C:ARG328 5.0 42.5 1.0
N C:SER323 5.0 53.2 1.0

Potassium binding site 4 out of 8 in 9i0m

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Potassium binding site 4 out of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) Saturating Atp+Imp-Bound Form, 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) Saturating Atp+Imp-Bound Form, Extended within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K602

b:85.0
occ:1.00
 O D:CYS325 2.7 66.0 1.0
O D:GLY320 2.7 60.1 1.0
O D:GLY322 2.7 61.3 1.0
O C:SER496 3.1 115.5 1.0
C D:CYS325 3.4 58.4 1.0
O C:GLU495 3.7 112.7 1.0
CB D:CYS325 3.7 56.8 1.0
C D:GLY322 3.9 57.4 1.0
C D:GLY320 3.9 55.0 1.0
C C:SER496 3.9 112.0 1.0
CA D:CYS325 3.9 56.5 1.0
N D:GLY322 4.1 53.4 1.0
N D:CYS325 4.1 56.5 1.0
C D:PRO321 4.2 54.1 1.0
O C:HIS497 4.3 129.4 1.0
SG D:CYS325 4.3 63.5 1.0
N D:THR326 4.4 52.7 1.0
C C:HIS497 4.5 129.0 1.0
CA D:PRO321 4.5 51.9 1.0
CA D:GLY322 4.5 52.9 1.0
CA C:SER496 4.5 106.4 1.0
CE1 C:HIS499 4.6 126.7 1.0
O D:PRO321 4.7 57.4 1.0
N D:PRO321 4.7 52.0 1.0
N C:PRO498 4.7 131.1 1.0
CA D:THR326 4.7 48.4 1.0
C C:GLU495 4.8 107.3 1.0
N C:HIS497 4.8 114.9 1.0
CA D:GLY320 4.9 47.7 1.0
ND1 C:HIS499 4.9 129.4 1.0
CA C:PRO498 4.9 133.3 1.0
N D:SER323 5.0 56.0 1.0
CA C:HIS497 5.0 122.7 1.0

Potassium binding site 5 out of 8 in 9i0m

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Potassium binding site 5 out of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) Saturating Atp+Imp-Bound Form, 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) Saturating Atp+Imp-Bound Form, Extended within 5.0Å range:
probe atom residue distance (Å) B Occ
E:K602

b:86.8
occ:1.00
 O E:GLY320 2.7 57.1 1.0
O E:GLY322 2.8 53.6 1.0
O H:SER496 2.9 91.9 1.0
O H:GLU495 2.9 84.1 1.0
O E:CYS325 3.1 58.7 1.0
C H:SER496 3.6 89.2 1.0
O H:HIS497 3.6 106.4 1.0
C E:GLY320 3.9 53.1 1.0
C E:CYS325 3.9 55.3 1.0
C E:GLY322 4.0 47.7 1.0
C H:HIS497 4.0 101.7 1.0
C E:PRO321 4.1 51.0 1.0
C H:GLU495 4.1 83.2 1.0
CA H:SER496 4.1 82.7 1.0
CB E:CYS325 4.1 50.6 1.0
N E:GLY322 4.1 50.8 1.0
CA E:PRO321 4.2 48.5 1.0
CD2 H:HIS499 4.4 101.8 1.0
NE2 H:HIS499 4.4 101.8 1.0
CA E:CYS325 4.4 51.6 1.0
N H:HIS497 4.4 91.4 1.0
O E:PRO321 4.4 52.0 1.0
N E:CYS325 4.4 52.2 1.0
N H:PRO498 4.5 100.9 1.0
N H:SER496 4.6 85.7 1.0
N E:PRO321 4.6 48.3 1.0
CA E:GLY322 4.7 46.2 1.0
CD E:ARG328 4.7 49.4 1.0
CA H:HIS497 4.7 96.4 1.0
CA H:PRO498 4.8 103.5 1.0
SG E:CYS325 4.8 58.7 1.0
N E:THR326 5.0 48.8 1.0
CA E:GLY320 5.0 48.8 1.0

Potassium binding site 6 out of 8 in 9i0m

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Potassium binding site 6 out of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) Saturating Atp+Imp-Bound Form, 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) Saturating Atp+Imp-Bound Form, Extended within 5.0Å range:
probe atom residue distance (Å) B Occ
F:K602

b:91.1
occ:1.00
 O F:GLY322 2.7 54.0 1.0
O F:CYS325 2.9 58.1 1.0
O E:GLU495 2.9 85.0 1.0
O F:GLY320 3.0 51.5 1.0
O E:SER496 3.0 85.1 1.0
O E:HIS497 3.5 98.3 1.0
C E:SER496 3.6 81.8 1.0
C E:HIS497 3.9 94.8 1.0
C F:CYS325 3.9 54.3 1.0
CE1 E:HIS499 3.9 100.2 1.0
C F:GLY322 3.9 46.6 1.0
ND1 E:HIS499 4.0 101.2 1.0
C E:GLU495 4.1 84.2 1.0
CB F:CYS325 4.1 52.1 1.0
C F:GLY320 4.2 48.7 1.0
C F:PRO321 4.2 48.2 1.0
CA E:SER496 4.2 76.8 1.0
N E:PRO498 4.2 92.7 1.0
N F:CYS325 4.3 47.8 1.0
N F:GLY322 4.3 48.1 1.0
CA F:CYS325 4.3 49.7 1.0
N E:HIS497 4.3 86.2 1.0
O F:PRO321 4.4 48.6 1.0
CA E:PRO498 4.4 96.3 1.0
CA F:PRO321 4.5 45.6 1.0
CA E:HIS497 4.6 89.9 1.0
N E:SER496 4.7 85.7 1.0
CA F:GLY322 4.7 43.1 1.0
N F:PRO321 4.8 47.2 1.0
N F:SER323 4.9 44.8 1.0
SG F:CYS325 4.9 71.2 1.0
CA F:SER323 4.9 45.1 1.0
N F:THR326 5.0 46.4 1.0
C F:SER323 5.0 49.3 1.0
CD F:ARG328 5.0 47.9 1.0

Potassium binding site 7 out of 8 in 9i0m

Go back to Potassium Binding Sites List in 9i0m
Potassium binding site 7 out of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) Saturating Atp+Imp-Bound Form, 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) Saturating Atp+Imp-Bound Form, Extended within 5.0Å range:
probe atom residue distance (Å) B Occ
G:K602

b:115.5
occ:1.00
 O G:CYS325 2.7 58.6 1.0
O F:SER496 2.7 125.7 1.0
O G:GLY320 2.9 49.8 1.0
O G:GLY322 3.0 56.7 1.0
O F:GLU495 3.5 112.0 1.0
C G:CYS325 3.5 55.3 1.0
C F:SER496 3.6 122.8 1.0
O F:HIS497 3.8 134.6 1.0
CB G:CYS325 3.8 50.1 1.0
C F:HIS497 4.1 132.7 1.0
CA G:CYS325 4.1 52.7 1.0
C G:GLY320 4.1 44.4 1.0
C G:GLY322 4.2 50.3 1.0
CA F:SER496 4.3 116.7 1.0
N G:CYS325 4.3 54.1 1.0
N F:HIS497 4.4 121.3 1.0
C G:PRO321 4.4 47.2 1.0
SG G:CYS325 4.5 62.6 1.0
N G:GLY322 4.5 46.3 1.0
N F:PRO498 4.5 135.3 1.0
N G:THR326 4.5 44.4 1.0
C F:GLU495 4.6 112.3 1.0
CA F:HIS497 4.6 125.9 1.0
CA G:PRO321 4.7 44.6 1.0
CD G:ARG328 4.7 40.1 1.0
O G:PRO321 4.8 49.7 1.0
NE2 F:HIS499 4.8 140.9 1.0
CD2 F:HIS499 4.8 135.8 1.0
CA F:PRO498 4.8 138.8 1.0
CA G:THR326 4.9 37.6 1.0
CA G:GLY322 4.9 44.1 1.0
N G:PRO321 4.9 44.3 1.0
N F:SER496 4.9 115.6 1.0

Potassium binding site 8 out of 8 in 9i0m

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Potassium binding site 8 out of 8 in the Mycobacterium Smegmatis Inosine Monophosphate Dehydrogenase (Impdh) Saturating Atp+Imp-Bound Form, 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) Saturating Atp+Imp-Bound Form, Extended within 5.0Å range:
probe atom residue distance (Å) B Occ
G:K603

b:120.3
occ:1.00
 O H:GLY322 2.7 59.9 1.0
O G:SER496 2.8 112.9 1.0
O G:GLU495 3.1 108.2 1.0
O H:CYS325 3.2 57.6 1.0
O G:HIS497 3.3 122.1 1.0
O H:GLY320 3.5 50.7 1.0
C G:SER496 3.5 108.7 1.0
C G:HIS497 3.6 120.8 1.0
C H:GLY322 3.9 55.1 1.0
N G:PRO498 3.9 122.8 1.0
C H:CYS325 4.0 57.5 1.0
CA G:PRO498 4.1 124.3 1.0
CD2 G:HIS499 4.1 124.9 1.0
NE2 G:HIS499 4.2 124.5 1.0
CA G:SER496 4.2 104.2 1.0
C G:GLU495 4.2 103.7 1.0
N G:HIS497 4.3 109.2 1.0
N H:CYS325 4.3 54.2 1.0
CB H:CYS325 4.3 52.0 1.0
C H:PRO321 4.4 50.6 1.0
CA G:HIS497 4.4 116.0 1.0
CA H:CYS325 4.5 53.7 1.0
N H:GLY322 4.5 53.6 1.0
O H:PRO321 4.5 53.9 1.0
O H:SER323 4.6 58.1 1.0
C H:GLY320 4.6 49.8 1.0
C H:SER323 4.7 55.8 1.0
CD G:PRO498 4.7 118.3 1.0
CA H:PRO321 4.7 46.7 1.0
CA H:SER323 4.7 50.8 1.0
N G:SER496 4.7 104.6 1.0
N H:SER323 4.8 50.4 1.0
CA H:GLY322 4.8 51.7 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 19:12:05 2025

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