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: Mon Aug 12 05:07:44 2024

Last articles

W in 8QLN
W in 8RJA
V in 8WTN
Te in 8QLN
Re in 9GHX
Rb in 8Z5C
Ni in 9C0T
Ni in 9C0S
Ni in 9GP1
Ni in 9FYO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy