Atomistry » Magnesium » PDB 1ofh-1oyj » 1olu
Atomistry »
  Magnesium »
    PDB 1ofh-1oyj »
      1olu »

Magnesium 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:

Potassium (K) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium 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 Magnesium atom.
In total only one binding site of Magnesium was 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:

Magnesium binding site 1 out of 1 in 1olu

Go back to Magnesium Binding Sites List in 1olu
Magnesium binding site 1 out of 1 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 Magnesium with other atoms in the Mg 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:Mg503

b:16.6
occ:1.00
 O A:TYR224 2.3 22.8 1.0
O13 A:TDP601 2.3 18.8 1.0
O23 A:TDP601 2.4 24.6 1.0
OD1 A:ASN222 2.4 21.9 1.0
OE1 A:GLU193 2.4 19.1 1.0
O A:HOH2163 2.5 22.1 1.0
OE2 A:GLU193 2.6 21.5 1.0
CD A:GLU193 2.8 18.1 1.0
CG A:ASN222 3.3 22.1 1.0
C A:TYR224 3.4 24.6 1.0
P2 A:TDP601 3.4 22.2 1.0
P1 A:TDP601 3.4 20.2 1.0
O11 A:TDP601 3.5 22.2 1.0
ND2 A:ASN222 3.6 22.1 1.0
N A:TYR224 4.1 25.1 1.0
O21 A:TDP601 4.1 26.3 1.0
O5G A:TDP601 4.1 20.9 1.0
N A:ALA225 4.2 24.0 1.0
CG A:GLU193 4.3 16.0 1.0
N A:ASN222 4.3 18.0 1.0
CA A:ALA225 4.3 22.9 1.0
N A:GLU193 4.3 12.8 1.0
CA A:TYR224 4.3 25.7 1.0
N A:GLY194 4.5 12.9 1.0
CB A:ASN222 4.6 21.8 1.0
O A:ARG220 4.6 16.1 1.0
O22 A:TDP601 4.6 22.6 1.0
O12 A:TDP601 4.6 14.9 1.0
O A:HOH2167 4.7 36.5 1.0
CB A:ALA225 4.8 21.8 1.0
CA A:ASN222 4.8 21.9 1.0
O A:HOH2278 4.8 24.5 1.0
N A:GLY223 4.8 23.9 1.0
CA A:GLY192 4.9 11.6 1.0
C A:ASN222 4.9 23.7 1.0
CB A:GLU193 5.0 13.6 1.0
C A:GLY192 5.0 11.0 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: Sun Aug 10 02:11:18 2025

Last articles

Mg in 4OZ6
Mg in 4OWU
Mg in 4OXD
Mg in 4OWQ
Mg in 4OWO
Mg in 4OWN
Mg in 4OWM
Mg in 4OTZ
Mg in 4OUI
Mg in 4OTT
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy