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Potassium in PDB 4z87: Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp

Enzymatic activity of Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp

All present enzymatic activity of Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp:
1.1.1.205;

Protein crystallography data

The structure of Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp, PDB code: 4z87 was solved by R.M.Buey, J.M.De Pereda, J.L.Revuelta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.03 / 2.25
Space group P 4
Cell size a, b, c (Å), α, β, γ (°) 122.042, 122.042, 147.613, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 22.5

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp (pdb code 4z87). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp, PDB code: 4z87:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 4z87

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Potassium binding site 1 out of 4 in the Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K605

b:47.2
occ:1.00
O A:GLY331 2.4 68.9 1.0
O A:GLY329 2.5 62.8 1.0
O A:CYS334 2.5 73.4 1.0
HB3 A:CYS334 3.3 78.6 1.0
C A:GLY329 3.5 56.5 1.0
C A:GLY331 3.5 61.7 1.0
C A:CYS334 3.6 69.3 1.0
H A:CYS334 3.6 79.9 1.0
N A:GLY331 3.8 49.0 1.0
H A:GLY331 3.9 58.8 1.0
C A:SER330 4.0 48.0 1.0
CB A:CYS334 4.1 65.5 1.0
N A:CYS334 4.1 66.6 1.0
HA2 A:GLY329 4.1 65.1 1.0
CA A:CYS334 4.1 68.2 1.0
HA A:SER330 4.1 57.8 1.0
CA A:GLY331 4.2 56.0 1.0
N A:SER330 4.3 48.7 1.0
O A:SER330 4.3 49.6 1.0
HA A:ILE335 4.4 79.2 1.0
CA A:SER330 4.4 48.1 1.0
CA A:GLY329 4.4 54.3 1.0
HA A:SER332 4.5 58.4 1.0
HA3 A:GLY331 4.6 67.2 1.0
N A:SER332 4.6 51.8 1.0
N A:ILE335 4.7 63.8 1.0
HA3 A:GLY329 4.8 65.1 1.0
HB2 A:CYS334 4.8 78.6 1.0
C A:SER332 4.8 50.4 1.0
SG A:CYS334 4.9 67.0 1.0
CA A:SER332 4.9 48.6 1.0
O A:SER332 5.0 50.4 1.0

Potassium binding site 2 out of 4 in 4z87

Go back to Potassium Binding Sites List in 4z87
Potassium binding site 2 out of 4 in the Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K605

b:51.7
occ:1.00
O B:GLY331 2.5 50.6 1.0
O B:CYS334 2.6 80.0 1.0
O B:GLY329 2.7 61.0 1.0
HB3 B:CYS334 3.4 95.6 1.0
C B:CYS334 3.5 77.1 1.0
H B:CYS334 3.6 91.2 1.0
C B:GLY331 3.6 53.5 1.0
C B:GLY329 3.7 53.4 1.0
N B:GLY331 4.0 43.1 1.0
H B:GLY331 4.0 51.8 1.0
CA B:CYS334 4.1 79.0 1.0
CB B:CYS334 4.1 79.7 1.0
HA B:ILE335 4.1 80.6 1.0
N B:CYS334 4.1 76.0 1.0
HA2 B:GLY329 4.2 60.4 1.0
C B:SER330 4.2 48.7 1.0
CA B:GLY331 4.3 48.9 1.0
HA B:SER330 4.4 60.6 1.0
N B:ILE335 4.4 69.1 1.0
CA B:GLY329 4.5 50.3 1.0
N B:SER330 4.5 51.7 1.0
HA3 B:GLY331 4.6 58.7 1.0
O B:SER330 4.6 55.1 1.0
CA B:SER330 4.6 50.5 1.0
N B:SER332 4.7 57.0 1.0
HA B:SER332 4.7 70.7 1.0
CA B:ILE335 4.8 67.2 1.0
SG B:CYS334 4.9 76.7 1.0
HA3 B:GLY329 4.9 60.4 1.0
HB2 B:CYS334 4.9 95.6 1.0
C B:SER332 4.9 63.6 1.0
O B:SER332 5.0 63.2 1.0

Potassium binding site 3 out of 4 in 4z87

Go back to Potassium Binding Sites List in 4z87
Potassium binding site 3 out of 4 in the Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K605

b:90.8
occ:1.00
O C:GLY331 2.4 60.6 1.0
O C:GLY329 2.6 72.5 1.0
O C:CYS334 2.7 83.8 1.0
HB3 C:CYS334 3.4 97.2 1.0
C C:GLY331 3.5 61.0 1.0
H C:CYS334 3.5 97.2 1.0
C C:GLY329 3.6 63.0 1.0
C C:CYS334 3.7 80.5 1.0
N C:GLY331 3.9 52.1 1.0
C C:SER330 4.0 56.0 1.0
H C:GLY331 4.0 62.5 1.0
N C:CYS334 4.1 81.0 1.0
CB C:CYS334 4.2 81.0 1.0
CA C:GLY331 4.2 56.0 1.0
CA C:CYS334 4.2 82.3 1.0
HA2 C:GLY329 4.2 73.3 1.0
HA C:SER330 4.3 67.9 1.0
O C:SER330 4.3 58.5 1.0
N C:SER330 4.4 57.0 1.0
CA C:SER330 4.5 56.6 1.0
HA C:ILE335 4.5 86.6 1.0
CA C:GLY329 4.5 61.0 1.0
HA C:SER332 4.5 74.1 1.0
N C:SER332 4.5 59.3 1.0
HA3 C:GLY331 4.5 67.2 1.0
C C:SER332 4.7 60.3 1.0
N C:ILE335 4.8 75.3 1.0
CA C:SER332 4.8 61.7 1.0
O C:SER332 4.9 57.1 1.0
HB2 C:CYS334 4.9 97.2 1.0
HA3 C:GLY329 4.9 73.3 1.0

Potassium binding site 4 out of 4 in 4z87

Go back to Potassium Binding Sites List in 4z87
Potassium binding site 4 out of 4 in the Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Structure of the Imp Dehydrogenase From Ashbya Gossypii Bound to Gdp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K604

b:62.9
occ:1.00
O D:CYS334 2.5 77.8 1.0
O D:GLY331 2.6 63.4 1.0
O D:GLY329 2.6 66.3 1.0
HB3 D:CYS334 3.1 85.8 0.5
HB2 D:CYS334 3.1 85.8 0.5
H D:CYS334 3.4 85.1 1.0
C D:CYS334 3.5 74.4 1.0
C D:GLY329 3.6 64.9 1.0
C D:GLY331 3.8 62.5 1.0
CB D:CYS334 3.9 71.5 0.5
CB D:CYS334 4.0 71.5 0.5
CA D:CYS334 4.0 73.2 0.5
HA2 D:GLY329 4.0 74.4 1.0
CA D:CYS334 4.1 73.2 0.5
N D:GLY331 4.1 58.9 1.0
H D:GLY331 4.1 70.7 1.0
N D:CYS334 4.2 70.9 1.0
C D:SER330 4.3 64.1 1.0
HA D:ILE335 4.3 89.4 1.0
HA D:SER330 4.4 80.7 1.0
CA D:GLY329 4.4 62.0 1.0
CA D:GLY331 4.5 61.3 1.0
N D:SER330 4.5 67.0 1.0
HB3 D:CYS334 4.5 85.8 0.5
HA D:SER332 4.6 73.2 1.0
HB2 D:CYS334 4.6 85.8 0.5
CA D:SER330 4.6 67.2 1.0
N D:ILE335 4.6 72.0 1.0
O D:SER330 4.7 66.0 1.0
HA3 D:GLY329 4.7 74.4 1.0
N D:SER332 4.8 62.7 1.0
O D:SER332 4.8 70.6 1.0
HA3 D:GLY331 4.8 73.6 1.0
SG D:CYS334 4.8 69.9 0.5
C D:SER332 4.9 65.3 1.0
HA D:CYS334 5.0 87.8 0.5
CA D:SER332 5.0 61.0 1.0

Reference:

R.M.Buey, R.Ledesma-Amaro, A.Velazquez-Campoy, M.Balsera, M.Chagoyen, J.M.De Pereda, J.L.Revuelta. Guanine Nucleotide Binding to the Bateman Domain Mediates the Allosteric Inhibition of Eukaryotic Imp Dehydrogenases. Nat Commun V. 6 8923 2015.
ISSN: ESSN 2041-1723
PubMed: 26558346
DOI: 10.1038/NCOMMS9923
Page generated: Mon Aug 12 12:45:02 2024

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