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Potassium in PDB 1dtw: Human Branched-Chain Alpha-Keto Acid Dehydrogenase

Enzymatic activity of Human Branched-Chain Alpha-Keto Acid Dehydrogenase

All present enzymatic activity of Human Branched-Chain Alpha-Keto Acid Dehydrogenase:
1.2.4.4;

Protein crystallography data

The structure of Human Branched-Chain Alpha-Keto Acid Dehydrogenase, PDB code: 1dtw was solved by A.Aevarsson, J.L.Chuang, R.M.Wynn, S.Turley, D.T.Chuang, W.G.J.Hol, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.70
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 143.760, 143.760, 69.160, 90.00, 90.00, 120.00
R / Rfree (%) 22.4 / 27.9

Other elements in 1dtw:

The structure of Human Branched-Chain Alpha-Keto Acid Dehydrogenase also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Human Branched-Chain Alpha-Keto Acid Dehydrogenase (pdb code 1dtw). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Human Branched-Chain Alpha-Keto Acid Dehydrogenase, PDB code: 1dtw:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1dtw

Go back to Potassium Binding Sites List in 1dtw
Potassium binding site 1 out of 2 in the Human Branched-Chain Alpha-Keto Acid Dehydrogenase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human Branched-Chain Alpha-Keto Acid Dehydrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K402

b:44.7
occ:1.00
OG A:SER161 2.9 33.3 1.0
O A:PRO163 3.0 31.7 1.0
OG1 A:THR166 3.1 29.9 1.0
O A:SER161 3.1 33.1 1.0
OE1 A:GLN167 3.2 29.4 1.0
CD A:GLN167 3.6 29.4 1.0
C A:SER161 3.8 33.1 1.0
NE2 A:GLN167 4.0 29.4 1.0
N A:GLN167 4.0 29.6 1.0
N A:SER161 4.0 33.7 1.0
CB A:SER161 4.0 33.4 1.0
C A:PRO163 4.1 31.6 1.0
CA A:SER161 4.1 33.4 1.0
CB A:GLN167 4.1 29.5 1.0
O A:GLY111 4.3 33.7 1.0
N A:THR166 4.3 30.1 1.0
CB A:THR166 4.4 29.9 1.0
CG A:GLN167 4.4 29.4 1.0
O A:HOH414 4.6 26.3 1.0
CA A:GLN167 4.7 29.5 1.0
N A:PRO163 4.7 32.1 1.0
CA A:THR166 4.7 29.9 1.0
C A:THR166 4.7 29.8 1.0
N A:ALA165 4.8 30.6 1.0
N A:SER162 4.8 32.9 1.0
OE2 B:GLU113 4.8 24.5 1.0
C A:SER162 4.8 32.3 1.0
CA A:LEU164 4.9 31.1 1.0
N A:LEU164 4.9 31.4 1.0
CA A:PRO163 4.9 31.9 1.0
CD A:PRO163 4.9 32.0 1.0
CG2 A:THR166 5.0 29.9 1.0
C A:LEU164 5.0 30.9 1.0

Potassium binding site 2 out of 2 in 1dtw

Go back to Potassium Binding Sites List in 1dtw
Potassium binding site 2 out of 2 in the Human Branched-Chain Alpha-Keto Acid Dehydrogenase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Human Branched-Chain Alpha-Keto Acid Dehydrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K343

b:49.9
occ:1.00
O B:HOH364 2.7 20.1 1.0
O B:GLY128 2.8 29.3 1.0
O B:ASN183 3.0 30.2 1.0
O B:ASP181 3.0 30.5 1.0
O B:CYS178 3.1 30.3 1.0
O B:LEU130 3.1 29.5 1.0
OG1 B:THR131 3.4 29.8 1.0
C B:ASN183 3.7 30.2 1.0
C B:GLY128 3.8 29.2 1.0
C B:LEU130 3.8 29.5 1.0
N B:LEU130 3.8 29.4 1.0
C B:ASP181 4.0 30.5 1.0
O B:ILE179 4.1 30.4 1.0
N B:ASN183 4.1 30.4 1.0
C B:SER129 4.2 29.3 1.0
CA B:SER129 4.2 29.3 1.0
N B:CYS185 4.2 29.9 1.0
C B:CYS178 4.2 30.3 1.0
CA B:PRO184 4.4 30.0 1.0
N B:PRO184 4.4 30.1 1.0
CA B:LEU130 4.4 29.4 1.0
C B:ILE179 4.4 30.4 1.0
N B:ASP181 4.4 30.5 1.0
N B:SER129 4.4 29.3 1.0
CB B:ASP181 4.5 30.4 1.0
CA B:ASP181 4.6 30.5 1.0
CA B:ASN183 4.6 30.2 1.0
CB B:CYS185 4.6 29.9 1.0
N B:THR131 4.6 29.6 1.0
CB B:THR131 4.6 29.7 1.0
SG B:CYS185 4.7 29.9 1.0
C B:PRO184 4.7 30.0 1.0
CA B:ILE179 4.7 30.4 1.0
CA B:GLY128 4.8 29.2 1.0
CA B:THR131 4.8 29.7 1.0
N B:LYS182 4.9 30.5 1.0
O B:SER129 4.9 29.3 1.0
N B:ILE179 4.9 30.3 1.0
C B:LYS182 5.0 30.4 1.0

Reference:

A.Aevarsson, J.L.Chuang, R.M.Wynn, S.Turley, D.T.Chuang, W.G.Hol. Crystal Structure of Human Branched-Chain Alpha-Ketoacid Dehydrogenase and the Molecular Basis of Multienzyme Complex Deficiency in Maple Syrup Urine Disease. Structure Fold.Des. V. 8 277 2000.
ISSN: ISSN 0969-2126
PubMed: 10745006
DOI: 10.1016/S0969-2126(00)00105-2
Page generated: Sun Dec 13 22:42:38 2020

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