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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

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