Potassium in PDB 8gil: L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi (Apo Form)
Enzymatic activity of L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi (Apo Form)
All present enzymatic activity of L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi (Apo Form):
1.1.1.103;
Protein crystallography data
The structure of L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi (Apo Form), PDB code: 8gil
was solved by
J.N.Faria,
G.F.Mercaldi,
M.Fagundes,
E.H.S.Bezerra,
A.T.Cordeiro,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.73 /
2.10
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
46.685,
81.834,
83.674,
90,
90.55,
90
|
R / Rfree (%)
|
20 /
25.8
|
Potassium Binding Sites:
The binding sites of Potassium atom in the L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi (Apo Form)
(pdb code 8gil). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the
L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi (Apo Form), PDB code: 8gil:
Jump to Potassium binding site number:
1;
2;
Potassium binding site 1 out
of 2 in 8gil
Go back to
Potassium Binding Sites List in 8gil
Potassium binding site 1 out
of 2 in the L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi (Apo Form)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi (Apo Form) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K601
b:77.0
occ:1.00
|
OE2
|
A:GLU221
|
2.9
|
28.4
|
1.0
|
O
|
A:PRO222
|
2.9
|
24.0
|
1.0
|
OD1
|
A:ASP293
|
2.9
|
27.1
|
1.0
|
O
|
A:TRP291
|
3.1
|
23.4
|
1.0
|
O
|
A:ALA288
|
3.1
|
28.5
|
1.0
|
O
|
A:PRO292
|
3.3
|
26.1
|
1.0
|
HD23
|
A:LEU223
|
3.3
|
27.8
|
1.0
|
HE3
|
A:LYS140
|
3.3
|
34.5
|
1.0
|
HA
|
A:ASP293
|
3.4
|
27.4
|
1.0
|
HD2
|
A:PRO222
|
3.6
|
23.8
|
1.0
|
C
|
A:PRO292
|
3.7
|
25.9
|
1.0
|
HA
|
A:HIS289
|
3.7
|
25.1
|
1.0
|
HG3
|
A:GLU221
|
3.8
|
29.2
|
1.0
|
HD22
|
A:LEU223
|
3.8
|
27.8
|
1.0
|
C
|
A:TRP291
|
3.9
|
24.4
|
1.0
|
N
|
A:ASP293
|
3.9
|
26.6
|
1.0
|
CD
|
A:GLU221
|
4.0
|
30.2
|
1.0
|
CD2
|
A:LEU223
|
4.0
|
27.8
|
1.0
|
H
|
A:TRP291
|
4.0
|
24.1
|
1.0
|
HB2
|
A:TRP291
|
4.1
|
22.7
|
1.0
|
C
|
A:PRO222
|
4.1
|
25.2
|
1.0
|
CG
|
A:ASP293
|
4.1
|
28.4
|
1.0
|
CA
|
A:ASP293
|
4.1
|
27.4
|
1.0
|
HZ2
|
A:LYS140
|
4.1
|
32.3
|
1.0
|
C
|
A:ALA288
|
4.2
|
24.9
|
1.0
|
CE
|
A:LYS140
|
4.2
|
34.5
|
1.0
|
HA
|
A:LEU223
|
4.3
|
23.1
|
1.0
|
HE2
|
A:LYS140
|
4.3
|
34.5
|
1.0
|
O
|
A:HIS289
|
4.3
|
21.9
|
1.0
|
HG
|
A:LEU223
|
4.4
|
24.1
|
1.0
|
CG
|
A:GLU221
|
4.4
|
29.2
|
1.0
|
CD
|
A:PRO222
|
4.4
|
23.8
|
1.0
|
CA
|
A:HIS289
|
4.5
|
25.1
|
1.0
|
C
|
A:HIS289
|
4.5
|
24.9
|
1.0
|
N
|
A:TRP291
|
4.5
|
24.1
|
1.0
|
H
|
A:ASP293
|
4.5
|
26.6
|
1.0
|
NZ
|
A:LYS140
|
4.5
|
32.3
|
1.0
|
CA
|
A:TRP291
|
4.6
|
25.0
|
1.0
|
N
|
A:PRO292
|
4.6
|
25.0
|
1.0
|
CA
|
A:PRO292
|
4.6
|
26.6
|
1.0
|
HB2
|
A:PRO222
|
4.6
|
24.0
|
1.0
|
N
|
A:PRO222
|
4.7
|
24.1
|
1.0
|
CB
|
A:ASP293
|
4.7
|
26.5
|
1.0
|
HD1
|
A:HIS289
|
4.7
|
32.7
|
0.0
|
HZ1
|
A:LYS140
|
4.7
|
32.3
|
1.0
|
CB
|
A:TRP291
|
4.7
|
22.7
|
1.0
|
HD21
|
A:LEU223
|
4.8
|
27.8
|
1.0
|
HA
|
A:PRO292
|
4.8
|
26.6
|
1.0
|
CG
|
A:LEU223
|
4.8
|
24.1
|
1.0
|
N
|
A:HIS289
|
4.8
|
25.2
|
1.0
|
HB1
|
A:ALA288
|
4.8
|
22.1
|
1.0
|
HG2
|
A:GLU221
|
4.9
|
29.2
|
1.0
|
HD3
|
A:PRO224
|
4.9
|
21.4
|
1.0
|
CA
|
A:PRO222
|
4.9
|
25.0
|
1.0
|
HB3
|
A:TRP291
|
5.0
|
22.7
|
1.0
|
|
Potassium binding site 2 out
of 2 in 8gil
Go back to
Potassium Binding Sites List in 8gil
Potassium binding site 2 out
of 2 in the L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi (Apo Form)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi (Apo Form) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K601
b:63.5
occ:1.00
|
O
|
B:TRP291
|
2.8
|
25.6
|
1.0
|
OE2
|
B:GLU221
|
2.9
|
32.2
|
1.0
|
OD1
|
B:ASP293
|
2.9
|
28.2
|
1.0
|
O
|
B:PRO222
|
3.0
|
27.6
|
1.0
|
O
|
B:ALA288
|
3.1
|
24.1
|
1.0
|
HE3
|
B:LYS140
|
3.2
|
28.8
|
1.0
|
O
|
B:PRO292
|
3.2
|
23.1
|
1.0
|
O
|
B:HOH703
|
3.3
|
24.9
|
1.0
|
HA
|
B:ASP293
|
3.3
|
26.4
|
1.0
|
HD23
|
B:LEU223
|
3.3
|
24.1
|
1.0
|
C
|
B:PRO292
|
3.5
|
25.4
|
1.0
|
HD2
|
B:PRO222
|
3.7
|
28.2
|
1.0
|
HA
|
B:HIS289
|
3.7
|
27.4
|
1.0
|
C
|
B:TRP291
|
3.7
|
25.1
|
1.0
|
HG3
|
B:GLU221
|
3.7
|
33.8
|
1.0
|
N
|
B:ASP293
|
3.8
|
24.4
|
1.0
|
HD22
|
B:LEU223
|
3.8
|
24.1
|
1.0
|
CD
|
B:GLU221
|
3.9
|
35.8
|
1.0
|
HZ2
|
B:LYS140
|
4.0
|
26.8
|
1.0
|
CA
|
B:ASP293
|
4.0
|
26.4
|
1.0
|
H
|
B:TRP291
|
4.0
|
29.0
|
1.0
|
CD2
|
B:LEU223
|
4.0
|
24.1
|
1.0
|
CE
|
B:LYS140
|
4.0
|
28.8
|
1.0
|
CG
|
B:ASP293
|
4.1
|
29.0
|
1.0
|
HB2
|
B:TRP291
|
4.1
|
27.1
|
1.0
|
C
|
B:PRO222
|
4.2
|
28.9
|
1.0
|
C
|
B:ALA288
|
4.2
|
27.1
|
1.0
|
HE2
|
B:LYS140
|
4.3
|
28.8
|
1.0
|
CG
|
B:GLU221
|
4.3
|
33.8
|
1.0
|
HA
|
B:LEU223
|
4.3
|
26.9
|
1.0
|
H
|
B:ASP293
|
4.3
|
24.4
|
1.0
|
NZ
|
B:LYS140
|
4.4
|
26.8
|
1.0
|
N
|
B:PRO292
|
4.4
|
23.8
|
1.0
|
CA
|
B:PRO292
|
4.4
|
24.7
|
1.0
|
HZ1
|
B:LYS140
|
4.4
|
26.8
|
1.0
|
N
|
B:TRP291
|
4.4
|
29.0
|
1.0
|
O
|
B:HIS289
|
4.5
|
25.9
|
1.0
|
CA
|
B:HIS289
|
4.5
|
27.4
|
1.0
|
HG
|
B:LEU223
|
4.5
|
28.2
|
1.0
|
CA
|
B:TRP291
|
4.5
|
25.5
|
1.0
|
CD
|
B:PRO222
|
4.5
|
28.2
|
1.0
|
HA
|
B:PRO292
|
4.5
|
24.7
|
1.0
|
C
|
B:HIS289
|
4.6
|
26.8
|
1.0
|
CB
|
B:ASP293
|
4.6
|
26.1
|
1.0
|
CB
|
B:TRP291
|
4.7
|
27.1
|
1.0
|
HG2
|
B:GLU221
|
4.7
|
33.8
|
1.0
|
HD21
|
B:LEU223
|
4.7
|
24.1
|
1.0
|
N
|
B:PRO222
|
4.7
|
26.3
|
1.0
|
HG2
|
B:LYS140
|
4.8
|
32.8
|
1.0
|
HG2
|
B:PRO222
|
4.8
|
26.5
|
1.0
|
HB3
|
B:LYS140
|
4.8
|
30.2
|
1.0
|
HB3
|
B:TRP291
|
4.8
|
27.1
|
1.0
|
N
|
B:HIS289
|
4.8
|
27.5
|
1.0
|
CG
|
B:LEU223
|
4.9
|
28.2
|
1.0
|
HB1
|
B:ALA288
|
5.0
|
26.6
|
1.0
|
|
Reference:
J.N.Faria,
G.F.Mercaldi,
M.Fagundes,
A.G.Eufrasio,
A.T.Cordeiro.
Structure, Allosteric Regulation and Metabolic Activity of L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi To Be Published.
Page generated: Mon Aug 12 23:50:27 2024
|