Atomistry » Manganese » PDB 1w2c-1xie » 1x7x
Atomistry »
  Manganese »
    PDB 1w2c-1xie »
      1x7x »

Manganese in PDB 1x7x: Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase

Enzymatic activity of Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase

All present enzymatic activity of Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase:
1.2.4.4;

Protein crystallography data

The structure of Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase, PDB code: 1x7x was solved by R.M.Wynn, M.Kato, 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) 50.00 / 2.10
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 145.672, 145.672, 69.236, 90.00, 90.00, 120.00
R / Rfree (%) 14.8 / 19

Other elements in 1x7x:

The structure of Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase also contains other interesting chemical elements:

Potassium (K) 2 atoms
Chlorine (Cl) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase (pdb code 1x7x). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase, PDB code: 1x7x:

Manganese binding site 1 out of 1 in 1x7x

Go back to Manganese Binding Sites List in 1x7x
Manganese binding site 1 out of 1 in the Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn703

b:16.2
occ:1.00
 O13 A:TDP801 2.1 11.5 1.0
O A:TYR224 2.2 19.4 1.0
OE1 A:GLU193 2.2 22.2 1.0
OD1 A:ASN222 2.2 26.8 1.0
O22 A:TDP801 2.2 13.1 1.0
O A:HOH811 2.4 14.2 1.0
CD A:GLU193 2.8 22.0 1.0
OE2 A:GLU193 2.9 21.8 1.0
CG A:ASN222 3.2 25.5 1.0
C A:TYR224 3.3 19.4 1.0
P1 A:TDP801 3.3 15.2 1.0
P2 A:TDP801 3.4 12.8 1.0
O11 A:TDP801 3.5 14.2 1.0
ND2 A:ASN222 3.6 21.2 1.0
N A:TYR224 4.0 21.2 1.0
O5G A:TDP801 4.1 14.5 1.0
O A:HOH980 4.1 38.0 1.0
N A:ALA225 4.1 19.0 1.0
O23 A:TDP801 4.1 12.1 1.0
CA A:TYR224 4.2 20.0 1.0
N A:GLU193 4.3 20.7 1.0
N A:ASN222 4.3 23.3 1.0
CA A:ALA225 4.3 18.8 1.0
CG A:GLU193 4.3 21.6 1.0
N A:GLY194 4.4 20.6 1.0
O A:ARG220 4.5 22.5 1.0
CB A:ASN222 4.5 24.5 1.0
O A:HOH859 4.5 21.9 1.0
O21 A:TDP801 4.6 13.7 1.0
O12 A:TDP801 4.6 16.5 1.0
N A:GLY223 4.7 23.7 1.0
CA A:ASN222 4.7 23.8 1.0
CB A:ALA225 4.8 17.6 1.0
C A:ASN222 4.8 24.5 1.0
CA A:GLY192 4.8 18.7 1.0
CB A:GLU193 4.8 19.4 1.0
O A:HOH839 4.9 18.9 1.0
CA A:GLU193 4.9 21.0 1.0
C A:GLY192 5.0 19.9 1.0

Reference:

R.M.Wynn, M.Kato, M.Machius, J.L.Chuang, J.Li, D.R.Tomchick, D.T.Chuang. Molecular Mechanism For Regulation of the Human Mitochondrial Branched-Chain Alpha-Ketoacid Dehydrogenase Complex By Phosphorylation Structure V. 12 2185 2004.
ISSN: ISSN 0969-2126
PubMed: 15576032
DOI: 10.1016/J.STR.2004.09.013
Page generated: Sat Oct 5 13:00:30 2024

Last articles

Ca in 5N7D
Ca in 5N5P
Ca in 5N6N
Ca in 5N5K
Ca in 5N5W
Ca in 5N5J
Ca in 5N4L
Ca in 5N3Y
Ca in 5N31
Ca in 5N3V
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy