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Potassium in PDB 8gjb: L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi in Complex with Nad and Acetate

Enzymatic activity of L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi in Complex with Nad and Acetate

All present enzymatic activity of L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi in Complex with Nad and Acetate:
1.1.1.103;

Protein crystallography data

The structure of L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi in Complex with Nad and Acetate, PDB code: 8gjb was solved by G.F.Mercaldi, J.N.Faria, 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) 47.32 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.274, 82.733, 84.384, 90, 90.45, 90
R / Rfree (%) 18 / 21

Potassium Binding Sites:

The binding sites of Potassium atom in the L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi in Complex with Nad and Acetate (pdb code 8gjb). 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 in Complex with Nad and Acetate, PDB code: 8gjb:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 8gjb

Go back to Potassium Binding Sites List in 8gjb
Potassium binding site 1 out of 2 in the L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi in Complex with Nad and Acetate


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 in Complex with Nad and Acetate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K403

b:50.4
occ:1.00
OE2 A:GLU221 2.7 22.6 1.0
O A:PRO222 2.8 20.4 1.0
O A:TRP291 2.9 18.0 1.0
OD1 A:ASP293 2.9 21.7 1.0
O A:ALA288 3.0 18.4 1.0
O A:PRO292 3.2 18.0 1.0
O A:HOH526 3.5 32.1 1.0
C A:PRO292 3.6 19.3 1.0
CD A:GLU221 3.8 23.2 1.0
C A:TRP291 3.8 19.6 1.0
N A:ASP293 3.9 21.3 1.0
CD2 A:LEU223 4.0 19.8 1.0
CA A:ASP293 4.0 21.5 1.0
C A:PRO222 4.1 20.2 1.0
C A:ALA288 4.1 21.6 1.0
CG A:ASP293 4.1 23.4 1.0
CE A:LYS140 4.2 32.1 1.0
CG A:GLU221 4.2 21.9 1.0
O A:HIS289 4.4 23.5 1.0
CA A:HIS289 4.4 21.0 1.0
CD A:PRO222 4.5 22.3 1.0
C A:HIS289 4.5 23.1 1.0
CA A:PRO292 4.5 18.8 1.0
N A:TRP291 4.6 19.7 1.0
N A:PRO292 4.6 16.8 1.0
CA A:TRP291 4.6 18.8 1.0
CB A:ASP293 4.6 20.8 1.0
N A:PRO222 4.7 21.5 1.0
N A:HIS289 4.7 19.7 1.0
CB A:TRP291 4.7 18.5 1.0
CG A:LEU223 4.7 20.4 1.0
NZ A:LYS140 4.8 30.3 1.0
OE1 A:GLU221 4.8 22.4 1.0
CA A:PRO222 4.9 20.0 1.0
CA A:LEU223 4.9 20.1 1.0
N A:LEU223 5.0 18.7 1.0

Potassium binding site 2 out of 2 in 8gjb

Go back to Potassium Binding Sites List in 8gjb
Potassium binding site 2 out of 2 in the L-Threonine 3-Dehydrogenase From Trypanosoma Cruzi in Complex with Nad and Acetate


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 in Complex with Nad and Acetate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K403

b:47.1
occ:1.00
O B:PRO222 2.7 18.8 1.0
OE2 B:GLU221 2.8 22.0 1.0
OD1 B:ASP293 2.8 25.8 1.0
O B:TRP291 2.9 19.2 1.0
O B:PRO292 3.0 17.2 1.0
O B:ALA288 3.1 18.0 1.0
O B:HOH510 3.5 29.3 1.0
C B:PRO292 3.6 18.1 1.0
N B:ASP293 3.8 17.8 1.0
C B:TRP291 3.8 19.2 1.0
CD B:GLU221 3.8 21.6 1.0
CA B:ASP293 3.9 20.0 1.0
CD2 B:LEU223 3.9 18.0 1.0
C B:PRO222 4.0 18.0 1.0
CG B:ASP293 4.0 25.2 1.0
CG B:GLU221 4.2 22.6 1.0
CE B:LYS140 4.2 27.0 1.0
C B:ALA288 4.2 19.1 1.0
O B:HIS289 4.5 21.2 1.0
CA B:HIS289 4.5 19.9 1.0
CB B:ASP293 4.5 21.7 1.0
CA B:PRO292 4.5 18.6 1.0
CD B:PRO222 4.6 17.0 1.0
N B:PRO292 4.6 18.3 1.0
CG B:LEU223 4.6 19.3 1.0
N B:TRP291 4.6 19.8 1.0
CA B:TRP291 4.6 18.8 1.0
C B:HIS289 4.7 20.9 1.0
NZ B:LYS140 4.7 32.1 1.0
N B:PRO222 4.7 18.1 1.0
CG B:PRO222 4.7 20.0 1.0
CB B:TRP291 4.8 17.7 1.0
CA B:LEU223 4.8 17.9 1.0
N B:HIS289 4.8 19.3 1.0
N B:LEU223 4.9 16.4 1.0
CA B:PRO222 4.9 18.1 1.0
OE1 B:GLU221 4.9 24.9 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 23:51:21 2024

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