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
Go back to
Potassium Binding Sites List in 4z87
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
|