Atomistry » Potassium » PDB 1o76-1pqo » 1olu
Atomistry »
  Potassium »
    PDB 1o76-1pqo »
      1olu »

Potassium in PDB 1olu: Roles of HIS291-Alpha and HIS146-Beta' in the Reductive Acylation Reaction Catalyzed By Human Branched-Chain Alpha-Ketoacid Dehydrogenase

Enzymatic activity of Roles of HIS291-Alpha and HIS146-Beta' in the Reductive Acylation Reaction Catalyzed By Human Branched-Chain Alpha-Ketoacid Dehydrogenase

All present enzymatic activity of Roles of HIS291-Alpha and HIS146-Beta' in the Reductive Acylation Reaction Catalyzed By Human Branched-Chain Alpha-Ketoacid Dehydrogenase:
1.2.4.4;

Protein crystallography data

The structure of Roles of HIS291-Alpha and HIS146-Beta' in the Reductive Acylation Reaction Catalyzed By Human Branched-Chain Alpha-Ketoacid Dehydrogenase, PDB code: 1olu was solved by R.M.Wynn, M.Machius, J.L.Chuang, J.Li, D.R.Tomchick, D.T.Chuang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.79 / 1.90
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 145.379, 145.379, 69.497, 90.00, 90.00, 120.00
R / Rfree (%) 16.1 / 20

Other elements in 1olu:

The structure of Roles of HIS291-Alpha and HIS146-Beta' in the Reductive Acylation Reaction Catalyzed By Human Branched-Chain Alpha-Ketoacid Dehydrogenase also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Roles of HIS291-Alpha and HIS146-Beta' in the Reductive Acylation Reaction Catalyzed By Human Branched-Chain Alpha-Ketoacid Dehydrogenase (pdb code 1olu). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Roles of HIS291-Alpha and HIS146-Beta' in the Reductive Acylation Reaction Catalyzed By Human Branched-Chain Alpha-Ketoacid Dehydrogenase, PDB code: 1olu:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1olu

Go back to Potassium Binding Sites List in 1olu
Potassium binding site 1 out of 2 in the Roles of HIS291-Alpha and HIS146-Beta' in the Reductive Acylation Reaction Catalyzed By Human Branched-Chain Alpha-Ketoacid Dehydrogenase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Roles of HIS291-Alpha and HIS146-Beta' in the Reductive Acylation Reaction Catalyzed By Human Branched-Chain Alpha-Ketoacid Dehydrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K501

b:21.9
occ:1.00
O A:HOH2083 2.7 11.9 1.0
O A:PRO163 2.7 12.0 1.0
O A:SER161 2.9 12.9 1.0
OE1 A:GLN112 2.9 22.6 1.0
OE1 A:GLN167 3.0 10.8 1.0
OG A:SER161 3.0 13.3 1.0
OG1 A:THR166 3.1 12.3 1.0
C A:SER161 3.7 13.4 1.0
CD A:GLN112 3.8 25.0 1.0
C A:PRO163 3.8 13.8 1.0
CD A:GLN167 3.9 11.6 1.0
NE2 A:GLN112 4.0 25.6 1.0
N A:SER161 4.1 12.4 1.0
CB A:SER161 4.2 12.1 1.0
O B:HOH2107 4.2 15.5 1.0
N A:GLN167 4.2 10.1 1.0
CA A:SER161 4.3 13.2 1.0
N A:THR166 4.3 8.8 1.0
N A:PRO163 4.4 13.1 1.0
CB A:GLN167 4.5 10.4 1.0
CB A:THR166 4.5 10.9 1.0
O A:GLY111 4.5 15.7 1.0
N A:ALA165 4.5 9.8 1.0
C A:SER162 4.5 12.8 1.0
CA A:LEU164 4.6 11.8 1.0
O A:HOH2136 4.6 14.0 1.0
N A:LEU164 4.6 12.0 1.0
CA A:PRO163 4.7 12.9 1.0
O A:HOH2084 4.7 14.0 1.0
C A:LEU164 4.7 10.1 1.0
N A:SER162 4.7 10.6 1.0
CG A:GLN167 4.7 9.8 1.0
CA A:THR166 4.8 10.4 1.0
NE2 A:GLN167 4.8 11.3 1.0
CD A:PRO163 4.8 12.2 1.0
O A:SER162 4.8 12.3 1.0
OE2 B:GLU113 4.9 13.0 1.0
C A:THR166 4.9 9.9 1.0
CA A:GLN167 5.0 10.3 1.0

Potassium binding site 2 out of 2 in 1olu

Go back to Potassium Binding Sites List in 1olu
Potassium binding site 2 out of 2 in the Roles of HIS291-Alpha and HIS146-Beta' in the Reductive Acylation Reaction Catalyzed By Human Branched-Chain Alpha-Ketoacid Dehydrogenase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Roles of HIS291-Alpha and HIS146-Beta' in the Reductive Acylation Reaction Catalyzed By Human Branched-Chain Alpha-Ketoacid Dehydrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K502

b:25.6
occ:1.00
O B:CYS178 2.8 12.9 1.0
O B:ASN183 2.8 11.4 1.0
O B:GLY128 2.8 13.3 1.0
O B:ASP181 3.0 12.7 1.0
O B:LEU130 3.0 10.3 1.0
O B:HOH2126 3.1 17.1 1.0
OG1 B:THR131 3.4 14.1 1.0
C B:LEU130 3.7 12.7 1.0
C B:ASN183 3.9 13.2 1.0
C B:ASP181 3.9 13.1 1.0
C B:CYS178 4.0 13.8 1.0
C B:GLY128 4.0 13.8 1.0
O B:ILE179 4.0 13.4 1.0
N B:LEU130 4.0 13.4 1.0
SG B:CYS185 4.0 16.3 1.0
N B:CYS185 4.2 8.9 1.0
C B:SER129 4.2 13.2 1.0
N B:ASN183 4.3 12.8 1.0
CA B:SER129 4.3 13.8 1.0
N B:ASP181 4.3 14.5 1.0
C B:ILE179 4.3 14.4 1.0
CB B:CYS185 4.4 13.4 1.0
CB B:ASP181 4.4 15.6 1.0
O B:HOH2159 4.4 26.2 1.0
CA B:ASP181 4.5 13.2 1.0
N B:THR131 4.5 11.4 1.0
CA B:PRO184 4.5 10.7 1.0
CA B:LEU130 4.5 11.7 1.0
CA B:ILE179 4.6 14.1 1.0
CB B:THR131 4.6 12.1 1.0
N B:PRO184 4.6 11.4 1.0
CA B:THR131 4.7 11.8 1.0
C B:PRO184 4.7 12.2 1.0
N B:SER129 4.7 12.1 1.0
N B:ILE179 4.7 13.0 1.0
CA B:ASN183 4.8 11.6 1.0
O B:SER129 4.8 12.2 1.0
N B:LYS182 4.9 10.7 1.0
CA B:CYS185 4.9 12.5 1.0
CA B:CYS178 5.0 14.3 1.0

Reference:

R.M.Wynn, M.Machius, J.L.Chuang, J.Li, D.R.Tomchick, D.T.Chuang. Roles of HIS291-Alpha and HIS146-Beta' in the Reductive Acylation Reaction Catalyzed By Human Branched-Chain Alpha-Ketoacid Dehydrogenase: Refined Phosphorylation Loop Structure in the Active Site. J.Biol.Chem. V. 278 43402 2003.
ISSN: ISSN 0021-9258
PubMed: 12902323
DOI: 10.1074/JBC.M306204200
Page generated: Sat Aug 9 02:24:14 2025

Last articles

Na in 7DJQ
Na in 7DJK
Na in 7DKM
Na in 7DJM
Na in 7DJL
Na in 7DJC
Na in 7DJJ
Na in 7DJ2
Na in 7DJ1
Na in 7DII
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy